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2nqd

Crystal structure of cysteine protease inhibitor, chagasin, in complex with human cathepsin L

Method: X-RAY DIFFRACTION Dmax: 79.1 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Chagasin

Trypanosoma cruzi

UniProt Q966X9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 2–110 Not recorded Cathepsin L × 1 （P07711） 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NA SODIUM ION × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 5.6；291 K；20% iso-Propanol, 20% PEG 4000, 0.1M Na Citrate pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 1.75 Å R-free 0.188

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 2NQD Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
2FO8 Solution structure of the Trypanosoma cruzi cysteine protease inhibitor chagasin Deposited 2006-01-13 Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 2–110（109 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5.6；298 K；Ionic strength (raw mmCIF value) 50 mM NaCl；Pressure 1
NMR sample composition 1.19 mM unlabeled chagasin | 90% H2O / 10% D2O; 20mM phosphate buffer
NMR sample composition 1.19 mM unlabeled chagasin | 100% D2O; 20mM phosphate buffer
NMR sample composition 0.52 mM U-15N chagasin | 90% H2O / 10% D2O; 20mM phosphate buffer
NMR sample composition 0.73 mM U-15N,13C chagasin | 100% D2O; 20mM phosphate buffer
NMR sample composition 0.3 mM U-15N,13C chagasin | 90% H2O / 10% D2O; 20mM phosphate buffer
Resolution not provided
2H7W Crystal structure of Chagasin, the endogenous cysteine-protease inhibitor from Trypanosoma cruzi Deposited 2006-06-05 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–110（110 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；291 K；protein: 15 mg/ml in 10 mM tris-Hcl, pH 7.4, 0.1 M sodium chloride. reservoir: 15% PEG 8000, 0.1M ammonium sulphate, 0.1M cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 291.0K
Resolution 1.70 Å R-free 0.238
2H7W Crystal structure of Chagasin, the endogenous cysteine-protease inhibitor from Trypanosoma cruzi Deposited 2006-06-05 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 1–110（110 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；291 K；protein: 15 mg/ml in 10 mM tris-Hcl, pH 7.4, 0.1 M sodium chloride. reservoir: 15% PEG 8000, 0.1M ammonium sulphate, 0.1M cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 291.0K
Resolution 1.70 Å R-free 0.238
2NNR Crystal structure of chagasin, cysteine protease inhibitor from Trypanosoma cruzi Deposited 2006-10-24 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–110（110 aa）
Not recorded SO4 SULFATE ION × 1 GOL GLYCEROL × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；291 K；1.5M Lithium Sulfate, 0.1M Hepes pH 8.5, protein concentration 8 mg/ml, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 1.70 Å R-free 0.216
2NNR Crystal structure of chagasin, cysteine protease inhibitor from Trypanosoma cruzi Deposited 2006-10-24 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 1–110（110 aa）
Not recorded GOL GLYCEROL × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；291 K；1.5M Lithium Sulfate, 0.1M Hepes pH 8.5, protein concentration 8 mg/ml, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 1.70 Å R-free 0.216
2OUL The Structure of Chagasin in Complex with a Cysteine Protease Clarifies the Binding Mode and Evolution of a New Inhibitor Family Deposited 2007-02-11 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–110（110 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；277 K；20% (v/v) PEG-300, 0.1 M Tris pH 8.5, 5% (w/v) PEG8000, and 10-15% (v/v) glycerol, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K, pH 7.00
Resolution 2.20 Å R-free 0.232
3CBJ Chagasin-Cathepsin B complex Deposited 2008-02-22 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–110（110 aa）
Not recorded PO4 PHOSPHATE ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；291 K；0.2 M ammonium dihydrogen phosphate, 20% PEG 3350, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 1.80 Å R-free 0.210
3CBJ Chagasin-Cathepsin B complex Deposited 2008-02-22 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–110（110 aa）
Not recorded PO4 PHOSPHATE ION × 8 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；291 K；0.2 M ammonium dihydrogen phosphate, 20% PEG 3350, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 1.80 Å R-free 0.210
3CBK chagasin-cathepsin B Deposited 2008-02-22 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–110（110 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.2；291 K；0.14M ammonium fluoride, 14% PEG 3350, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 2.67 Å R-free 0.242
3E1Z Crystal structure of the parasite protesase inhibitor chagasin in complex with papain Deposited 2008-08-05 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–110（110 aa）
Not recorded ZN ZINC ION × 1 FMT FORMIC ACID × 10 ACY ACETIC ACID × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；291 K；2.0M ammonium formate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 1.86 Å R-free 0.208

7 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CHAG_TRYCR
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–109； UniProt 2–110

Cathepsin L

Homo sapiens

UniProt P07711

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric（2） Consistent with protein copy count Chain B； UniProt 113–333 Fragment：residues 1-220 Mutation：C25A Chagasin × 1 （Q966X9） 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NA SODIUM ION × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 5.6；291 K；20% iso-Propanol, 20% PEG 4000, 0.1M Na Citrate pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 1.75 Å R-free 0.188

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 2NQD Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1CJL CRYSTAL STRUCTURE OF A CYSTEINE PROTEASE PROFORM Deposited 1996-07-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 22–333（312 aa）
Mutation：F(78P)L, C25S, T110A, E176G, D178G No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.8；1.4M (NA,K)PO4, PH 7.8
Resolution 2.20 Å R-free 0.241
1CS8 CRYSTAL STRUCTURE OF PROCATHEPSIN L Deposited 1999-08-17 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 18–333（316 aa）
Mutation：T110A Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions MICROBATCH；pH 7.8；293.2 K；Na,K,Phosphate, pH 7.8, MICROBATCH, temperature 20.2K
Resolution 1.80 Å R-free 0.229
1ICF CRYSTAL STRUCTURE OF MHC CLASS II ASSOCIATED P41 II FRAGMENT IN COMPLEX WITH CATHEPSIN L Deposited 1999-01-07 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain A 114–288（175 aa）
Chain B 292–333（42 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.1；SITTING DROP VAPOR DIFFUSION METHOD RESERVOIR CONTAINED 1ML OF 0.2 M NA- ACETATE TRIHYDRATE, 30% W/V PEG 8K AND 0.1M MES, PH 6.1. DROP WAS COMPOSED OF 2 MICRO L OF RESERVOIR SOLUTION AND 2 MICRO L OF THE COMPLEX (10 MG/ML) IN 20MM NA-ACETATE AND 1MM EDTA, PH 5.0.
Resolution 2.00 Å R-free 0.213
1ICF CRYSTAL STRUCTURE OF MHC CLASS II ASSOCIATED P41 II FRAGMENT IN COMPLEX WITH CATHEPSIN L Deposited 1999-01-07 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain C 114–288（175 aa）
Chain D 292–333（42 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.1；SITTING DROP VAPOR DIFFUSION METHOD RESERVOIR CONTAINED 1ML OF 0.2 M NA- ACETATE TRIHYDRATE, 30% W/V PEG 8K AND 0.1M MES, PH 6.1. DROP WAS COMPOSED OF 2 MICRO L OF RESERVOIR SOLUTION AND 2 MICRO L OF THE COMPLEX (10 MG/ML) IN 20MM NA-ACETATE AND 1MM EDTA, PH 5.0.
Resolution 2.00 Å R-free 0.213
1ICF CRYSTAL STRUCTURE OF MHC CLASS II ASSOCIATED P41 II FRAGMENT IN COMPLEX WITH CATHEPSIN L Deposited 1999-01-07 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric
Chain A 114–288（175 aa）
Chain B 292–333（42 aa）
Chain C 114–288（175 aa）
Chain D 292–333（42 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.1；SITTING DROP VAPOR DIFFUSION METHOD RESERVOIR CONTAINED 1ML OF 0.2 M NA- ACETATE TRIHYDRATE, 30% W/V PEG 8K AND 0.1M MES, PH 6.1. DROP WAS COMPOSED OF 2 MICRO L OF RESERVOIR SOLUTION AND 2 MICRO L OF THE COMPLEX (10 MG/ML) IN 20MM NA-ACETATE AND 1MM EDTA, PH 5.0.
Resolution 2.00 Å R-free 0.213
1MHW Design of non-covalent inhibitors of human cathepsin L. From the 96-residue proregion to optimized tripeptides Deposited 2002-08-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 114–288（175 aa） Fragment：HEAVY CHAIN (residues 114-288)
Chain C 292–333（42 aa） Fragment：LIGHT CHAIN (residues 292-333)
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.2；293 K；PEG 8K, Na Citrate, LiSo4, Isoproponal, pH 4.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.90 Å R-free 0.230
1MHW Design of non-covalent inhibitors of human cathepsin L. From the 96-residue proregion to optimized tripeptides Deposited 2002-08-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 114–288（175 aa） Fragment：HEAVY CHAIN (residues 114-288)
Chain D 292–333（42 aa） Fragment：LIGHT CHAIN (residues 292-333)
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.2；293 K；PEG 8K, Na Citrate, LiSo4, Isoproponal, pH 4.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.90 Å R-free 0.230
2VHS Cathsilicatein, a chimera Deposited 2007-11-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 114–285（172 aa）
Chain A 294–333（40 aa）
Chain B 114–285（172 aa）
Chain B 294–333（40 aa）
Chain C 114–285（172 aa）
Chain C 294–333（40 aa）
Chain D 114–285（172 aa）
Chain D 294–333（40 aa）
Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES SO4 SULFATE ION × 8 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；pH 6
Resolution 1.50 Å R-free 0.220
2XU1 CATHEPSIN L WITH A NITRILE INHIBITOR Deposited 2010-10-14 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–333（220 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 114-333
Mutation：YES 424 (2S,4R)-1-[1-(4-chlorophenyl)cyclopropyl]carbonyl-4-(2-chlorophenyl)sulfonyl-N-[1-(iminomethyl)cyclopropyl]pyrrolidine-2-carboxamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 4；20% PEG 2000, PH 4
Resolution 1.45 Å R-free 0.272
2XU1 CATHEPSIN L WITH A NITRILE INHIBITOR Deposited 2010-10-14 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 114–333（220 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 114-333
Mutation：YES 424 (2S,4R)-1-[1-(4-chlorophenyl)cyclopropyl]carbonyl-4-(2-chlorophenyl)sulfonyl-N-[1-(iminomethyl)cyclopropyl]pyrrolidine-2-carboxamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 4；20% PEG 2000, PH 4
Resolution 1.45 Å R-free 0.272
2XU1 CATHEPSIN L WITH A NITRILE INHIBITOR Deposited 2010-10-14 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 114–333（220 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 114-333
Mutation：YES 424 (2S,4R)-1-[1-(4-chlorophenyl)cyclopropyl]carbonyl-4-(2-chlorophenyl)sulfonyl-N-[1-(iminomethyl)cyclopropyl]pyrrolidine-2-carboxamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 4；20% PEG 2000, PH 4
Resolution 1.45 Å R-free 0.272
2XU1 CATHEPSIN L WITH A NITRILE INHIBITOR Deposited 2010-10-14 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 114–333（220 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 114-333
Mutation：YES 424 (2S,4R)-1-[1-(4-chlorophenyl)cyclopropyl]carbonyl-4-(2-chlorophenyl)sulfonyl-N-[1-(iminomethyl)cyclopropyl]pyrrolidine-2-carboxamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 4；20% PEG 2000, PH 4
Resolution 1.45 Å R-free 0.272
2XU3 CATHEPSIN L WITH A NITRILE INHIBITOR Deposited 2010-10-14 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–333（220 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 114-333
Not recorded XU3 (2S,4R)-4-(2-chlorophenyl)sulfonyl-1-[1-(5-chlorothiophen-2-yl)cyclopropyl]carbonyl-N-[1-(iminomethyl)cyclopropyl]pyrrolidine-2-carboxamide × 1 BTB 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 2 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.2；0.1 M CITRIC ACID PH 3.5 25 % PEG 3350
Resolution 0.90 Å R-free 0.155
2XU4 CATHEPSIN L WITH A NITRILE INHIBITOR Deposited 2010-10-14 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–333（220 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 114-333
Not recorded DJT (2S,4R)-4-(2-chlorophenyl)sulfonyl-1-[1-(4-fluorophenyl)cyclopropyl]carbonyl-N-[1-(iminomethyl)cyclopropyl]pyrrolidine-2-carboxamide × 1 GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 3.5；0.1 M CITRIC ACID PH 3.5, 25 % PEG 3350
Resolution 1.12 Å R-free 0.167
2XU5 CATHEPSIN L WITH A NITRILE INHIBITOR Deposited 2010-10-14 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–333（220 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 114-333
Not recorded XU5 (2S,4R)-4-(2-chlorophenyl)sulfonyl-N-[1-(iminomethyl)cyclopropyl]-1-[1-(4-methylphenyl)cyclopropyl]carbonyl-pyrrolidine-2-carboxamide × 1 GOL GLYCEROL × 1 FLC CITRATE ANION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 3.5；0.1 M CITRIC ACID PH 3.5, 25 % PEG 3350
Resolution 1.60 Å R-free 0.276
2YJ2 CATHEPSIN L WITH A NITRILE INHIBITOR Deposited 2011-05-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–333（220 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 114-333
Not recorded YJ2 (2S,4R)-1-[1-(4-BROMOPHENYL)CYCLOPROPYL]CARBONYL-4-(2-CHLOROPHENYL)SULFONYL-N-[1-(IMINOMETHYL)CYCLOPROPYL]PYRROLIDINE-2-CARBOXAMIDE × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；0.1M BIS-TRIS PH 6.5, 25 % PEG 3350
Resolution 1.15 Å R-free 0.179
2YJ8 CATHEPSIN L WITH A NITRILE INHIBITOR Deposited 2011-05-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–333（220 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 114-333
Not recorded YJ8 (2S,4R)-4-(2-chlorophenyl)sulfonyl-N-[1-(iminomethyl)cyclopropyl]-1-[1-(4-iodophenyl)cyclopropyl]carbonyl-pyrrolidine-2-carboxamide × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 5.5；0.1 M BIS-TRIS PH 5.5, 0.2M SODIUM ACETATE, 25 % PEG 3350
Resolution 1.30 Å R-free 0.182
2YJ9 CATHEPSIN L WITH A NITRILE INHIBITOR Deposited 2011-05-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–333（220 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 114-333
Not recorded YJ9 (2S,4R)-4-(2-chlorophenyl)sulfonyl-N-[1-(iminomethyl)cyclopropyl]-1-[1-[4-(trifluoromethyl)phenyl]cyclopropyl]carbonyl-pyrrolidine-2-carboxamide × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；0.1 M BIS-TRIS 6.5, 20% PEG MME 5000
Resolution 1.35 Å R-free 0.201
2YJB CATHEPSIN L WITH A NITRILE INHIBITOR Deposited 2011-05-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–333（220 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 114-333
Not recorded YJ9 (2S,4R)-4-(2-chlorophenyl)sulfonyl-N-[1-(iminomethyl)cyclopropyl]-1-[1-[4-(trifluoromethyl)phenyl]cyclopropyl]carbonyl-pyrrolidine-2-carboxamide × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；0.1 M BIS-TRIS PH 6.5, 0.2 M NACL, 25% PEG 3350
Resolution 1.40 Å R-free 0.218
2YJC CATHEPSIN L WITH A NITRILE INHIBITOR Deposited 2011-05-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–333（220 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 114-333
Not recorded 424 (2S,4R)-1-[1-(4-chlorophenyl)cyclopropyl]carbonyl-4-(2-chlorophenyl)sulfonyl-N-[1-(iminomethyl)cyclopropyl]pyrrolidine-2-carboxamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions 0.1M MAGNESIUM FORMATE, 15 % PEG 3350
Resolution 1.14 Å R-free 0.184
3BC3 Exploring inhibitor binding at the S subsites of cathepsin L Deposited 2007-11-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–333（220 aa） Fragment：UNp residues 114-333
Non-standard monomer：Yes (specific site not provided by mmCIF) OPT S-benzyl-N-(biphenyl-4-ylacetyl)-L-cysteinyl-N~5~-(diaminomethyl)-D-ornithyl-N-(2-phenylethyl)-L-tyrosinamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；17%(w/v) Polyethylene glycol 8000, 0.2M ammonium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.20 Å R-free 0.234
3BC3 Exploring inhibitor binding at the S subsites of cathepsin L Deposited 2007-11-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 114–333（220 aa） Fragment：UNp residues 114-333
Non-standard monomer：Yes (specific site not provided by mmCIF) OPT S-benzyl-N-(biphenyl-4-ylacetyl)-L-cysteinyl-N~5~-(diaminomethyl)-D-ornithyl-N-(2-phenylethyl)-L-tyrosinamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；17%(w/v) Polyethylene glycol 8000, 0.2M ammonium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.20 Å R-free 0.234
3H89 A combined crystallographic and molecular dynamics study of cathepsin-L retro-binding inhibitors(compound 4) Deposited 2009-04-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–333（220 aa） Fragment：Cathepsin L Heavy Chain and Light Chain, UNP residues 114-333
Not recorded NSX N~2~,N~6~-bis(biphenyl-4-ylacetyl)-L-lysyl-D-arginyl-N-(2-phenylethyl)-L-tyrosinamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；VAPOR DIFFUSION, HANGING DROP
Resolution 2.50 Å R-free 0.280
3H89 A combined crystallographic and molecular dynamics study of cathepsin-L retro-binding inhibitors(compound 4) Deposited 2009-04-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 114–333（220 aa） Fragment：Cathepsin L Heavy Chain and Light Chain, UNP residues 114-333
Not recorded NSX N~2~,N~6~-bis(biphenyl-4-ylacetyl)-L-lysyl-D-arginyl-N-(2-phenylethyl)-L-tyrosinamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；VAPOR DIFFUSION, HANGING DROP
Resolution 2.50 Å R-free 0.280
3H89 A combined crystallographic and molecular dynamics study of cathepsin-L retro-binding inhibitors(compound 4) Deposited 2009-04-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 114–333（220 aa） Fragment：Cathepsin L Heavy Chain and Light Chain, UNP residues 114-333
Not recorded NSX N~2~,N~6~-bis(biphenyl-4-ylacetyl)-L-lysyl-D-arginyl-N-(2-phenylethyl)-L-tyrosinamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；VAPOR DIFFUSION, HANGING DROP
Resolution 2.50 Å R-free 0.280
3H89 A combined crystallographic and molecular dynamics study of cathepsin-L retro-binding inhibitors(compound 4) Deposited 2009-04-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 114–333（220 aa） Fragment：Cathepsin L Heavy Chain and Light Chain, UNP residues 114-333
Not recorded NSX N~2~,N~6~-bis(biphenyl-4-ylacetyl)-L-lysyl-D-arginyl-N-(2-phenylethyl)-L-tyrosinamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；VAPOR DIFFUSION, HANGING DROP
Resolution 2.50 Å R-free 0.280
3H89 A combined crystallographic and molecular dynamics study of cathepsin-L retro-binding inhibitors(compound 4) Deposited 2009-04-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain E 114–333（220 aa） Fragment：Cathepsin L Heavy Chain and Light Chain, UNP residues 114-333
Not recorded NSX N~2~,N~6~-bis(biphenyl-4-ylacetyl)-L-lysyl-D-arginyl-N-(2-phenylethyl)-L-tyrosinamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；VAPOR DIFFUSION, HANGING DROP
Resolution 2.50 Å R-free 0.280
3H89 A combined crystallographic and molecular dynamics study of cathepsin-L retro-binding inhibitors(compound 4) Deposited 2009-04-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 6 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain F 114–333（220 aa） Fragment：Cathepsin L Heavy Chain and Light Chain, UNP residues 114-333
Not recorded NSX N~2~,N~6~-bis(biphenyl-4-ylacetyl)-L-lysyl-D-arginyl-N-(2-phenylethyl)-L-tyrosinamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；VAPOR DIFFUSION, HANGING DROP
Resolution 2.50 Å R-free 0.280
3H8B A combined crystallographic and molecular dynamics study of cathepsin-L retro-binding inhibitors(compound 9) Deposited 2009-04-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–333（220 aa） Fragment：Cathepsin L Heavy Chain and Light Chain, UNP residues 114-333
Not recorded NSY N~2~,N~6~-bis(biphenyl-4-ylacetyl)-L-lysyl-D-arginyl-N-(2-phenylethyl)-L-phenylalaninamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；VAPOR DIFFUSION, HANGING DROP
Resolution 1.80 Å R-free 0.250
3H8B A combined crystallographic and molecular dynamics study of cathepsin-L retro-binding inhibitors(compound 9) Deposited 2009-04-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 114–333（220 aa） Fragment：Cathepsin L Heavy Chain and Light Chain, UNP residues 114-333
Not recorded NSY N~2~,N~6~-bis(biphenyl-4-ylacetyl)-L-lysyl-D-arginyl-N-(2-phenylethyl)-L-phenylalaninamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；VAPOR DIFFUSION, HANGING DROP
Resolution 1.80 Å R-free 0.250
3H8B A combined crystallographic and molecular dynamics study of cathepsin-L retro-binding inhibitors(compound 9) Deposited 2009-04-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 114–333（220 aa） Fragment：Cathepsin L Heavy Chain and Light Chain, UNP residues 114-333
Not recorded NSY N~2~,N~6~-bis(biphenyl-4-ylacetyl)-L-lysyl-D-arginyl-N-(2-phenylethyl)-L-phenylalaninamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；VAPOR DIFFUSION, HANGING DROP
Resolution 1.80 Å R-free 0.250
3H8B A combined crystallographic and molecular dynamics study of cathepsin-L retro-binding inhibitors(compound 9) Deposited 2009-04-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 114–333（220 aa） Fragment：Cathepsin L Heavy Chain and Light Chain, UNP residues 114-333
Not recorded NSY N~2~,N~6~-bis(biphenyl-4-ylacetyl)-L-lysyl-D-arginyl-N-(2-phenylethyl)-L-phenylalaninamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；VAPOR DIFFUSION, HANGING DROP
Resolution 1.80 Å R-free 0.250
3H8B A combined crystallographic and molecular dynamics study of cathepsin-L retro-binding inhibitors(compound 9) Deposited 2009-04-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain E 114–333（220 aa） Fragment：Cathepsin L Heavy Chain and Light Chain, UNP residues 114-333
Not recorded NSY N~2~,N~6~-bis(biphenyl-4-ylacetyl)-L-lysyl-D-arginyl-N-(2-phenylethyl)-L-phenylalaninamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；VAPOR DIFFUSION, HANGING DROP
Resolution 1.80 Å R-free 0.250
3H8B A combined crystallographic and molecular dynamics study of cathepsin-L retro-binding inhibitors(compound 9) Deposited 2009-04-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 6 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain F 114–333（220 aa） Fragment：Cathepsin L Heavy Chain and Light Chain, UNP residues 114-333
Not recorded NSY N~2~,N~6~-bis(biphenyl-4-ylacetyl)-L-lysyl-D-arginyl-N-(2-phenylethyl)-L-phenylalaninamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；VAPOR DIFFUSION, HANGING DROP
Resolution 1.80 Å R-free 0.250
3H8C A combined crystallographic and molecular dynamics study of cathepsin-L retro-binding inhibitors (compound 14) Deposited 2009-04-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–333（220 aa） Fragment：Cathepsin L Heavy Chain and Light Chain, UNP residues 114-333
Non-standard monomer：Yes (specific site not provided by mmCIF) NSZ N-(biphenyl-4-ylacetyl)-S-methyl-L-cysteinyl-D-arginyl-N-(2-phenylethyl)-L-phenylalaninamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；VAPOR DIFFUSION, HANGING DROP
Resolution 2.50 Å R-free 0.292
3H8C A combined crystallographic and molecular dynamics study of cathepsin-L retro-binding inhibitors (compound 14) Deposited 2009-04-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 114–333（220 aa） Fragment：Cathepsin L Heavy Chain and Light Chain, UNP residues 114-333
Non-standard monomer：Yes (specific site not provided by mmCIF) NSZ N-(biphenyl-4-ylacetyl)-S-methyl-L-cysteinyl-D-arginyl-N-(2-phenylethyl)-L-phenylalaninamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；VAPOR DIFFUSION, HANGING DROP
Resolution 2.50 Å R-free 0.292
3HHA Crystal structure of cathepsin L in complex with AZ12878478 Deposited 2009-05-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–333（220 aa） Fragment：Heavy chain and light chain: UNP residues 76-333
Mutation：T223A NOW Nalpha-[(3-tert-butyl-1-methyl-1H-pyrazol-5-yl)carbonyl]-N-[(2Z)-2-iminoethyl]-3-methyl-L-phenylalaninamide × 1 PG4 TETRAETHYLENE GLYCOL × 1 ACT ACETATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 7.4；293 K；PEG, pH 7.4, VAPOR DIFFUSION, temperature 293K
Resolution 1.27 Å R-free 0.152
3HHA Crystal structure of cathepsin L in complex with AZ12878478 Deposited 2009-05-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 114–333（220 aa） Fragment：Heavy chain and light chain: UNP residues 76-333
Mutation：T223A NOW Nalpha-[(3-tert-butyl-1-methyl-1H-pyrazol-5-yl)carbonyl]-N-[(2Z)-2-iminoethyl]-3-methyl-L-phenylalaninamide × 1 PGE TRIETHYLENE GLYCOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 7.4；293 K；PEG, pH 7.4, VAPOR DIFFUSION, temperature 293K
Resolution 1.27 Å R-free 0.152
3HHA Crystal structure of cathepsin L in complex with AZ12878478 Deposited 2009-05-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 114–333（220 aa） Fragment：Heavy chain and light chain: UNP residues 76-333
Mutation：T223A NOW Nalpha-[(3-tert-butyl-1-methyl-1H-pyrazol-5-yl)carbonyl]-N-[(2Z)-2-iminoethyl]-3-methyl-L-phenylalaninamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 7.4；293 K；PEG, pH 7.4, VAPOR DIFFUSION, temperature 293K
Resolution 1.27 Å R-free 0.152
3HHA Crystal structure of cathepsin L in complex with AZ12878478 Deposited 2009-05-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 114–333（220 aa） Fragment：Heavy chain and light chain: UNP residues 76-333
Mutation：T223A NOW Nalpha-[(3-tert-butyl-1-methyl-1H-pyrazol-5-yl)carbonyl]-N-[(2Z)-2-iminoethyl]-3-methyl-L-phenylalaninamide × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 7.4；293 K；PEG, pH 7.4, VAPOR DIFFUSION, temperature 293K
Resolution 1.27 Å R-free 0.152
3HWN CATHEPSIN L with AZ13010160 Deposited 2009-06-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 76–333（258 aa） Fragment：PROTEASE
Not recorded BD3 Nalpha-[(3-tert-butyl-1-methyl-1H-pyrazol-5-yl)carbonyl]-N-[(2E)-2-iminoethyl]-3-{5-[(Z)-iminomethyl]-1,3,4-oxadiazol-2-yl}-L-phenylalaninamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.4；298 K；PEG, pH 7.4, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Resolution 2.33 Å R-free 0.347
3HWN CATHEPSIN L with AZ13010160 Deposited 2009-06-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 76–333（258 aa） Fragment：PROTEASE
Not recorded BD3 Nalpha-[(3-tert-butyl-1-methyl-1H-pyrazol-5-yl)carbonyl]-N-[(2E)-2-iminoethyl]-3-{5-[(Z)-iminomethyl]-1,3,4-oxadiazol-2-yl}-L-phenylalaninamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.4；298 K；PEG, pH 7.4, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Resolution 2.33 Å R-free 0.347
3HWN CATHEPSIN L with AZ13010160 Deposited 2009-06-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 76–333（258 aa） Fragment：PROTEASE
Not recorded BD3 Nalpha-[(3-tert-butyl-1-methyl-1H-pyrazol-5-yl)carbonyl]-N-[(2E)-2-iminoethyl]-3-{5-[(Z)-iminomethyl]-1,3,4-oxadiazol-2-yl}-L-phenylalaninamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.4；298 K；PEG, pH 7.4, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Resolution 2.33 Å R-free 0.347
3HWN CATHEPSIN L with AZ13010160 Deposited 2009-06-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 76–333（258 aa） Fragment：PROTEASE
Not recorded BD3 Nalpha-[(3-tert-butyl-1-methyl-1H-pyrazol-5-yl)carbonyl]-N-[(2E)-2-iminoethyl]-3-{5-[(Z)-iminomethyl]-1,3,4-oxadiazol-2-yl}-L-phenylalaninamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.4；298 K；PEG, pH 7.4, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Resolution 2.33 Å R-free 0.347
3IV2 Crystal structure of mature apo-Cathepsin L C25A mutant Deposited 2009-08-31 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 114–333（220 aa） Fragment：Mature protein: UNP residues 114-333
Chain B 114–333（220 aa） Fragment：Mature protein: UNP residues 114-333
Mutation：C138A Mutation：C138A NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 GOL GLYCEROL × 5 SO4 SULFATE ION × 4 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.6；293 K；0.2 M Ammonium sulfate, 0.1 M Sodium acetate trihydrate pH 4.6, 30% PEG MME 2000, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.20 Å R-free 0.244
3IV2 Crystal structure of mature apo-Cathepsin L C25A mutant Deposited 2009-08-31 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 114–333（220 aa） Fragment：Mature protein: UNP residues 114-333
Chain B 114–333（220 aa） Fragment：Mature protein: UNP residues 114-333
Mutation：C138A Mutation：C138A NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 GOL GLYCEROL × 5 SO4 SULFATE ION × 4 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.6；293 K；0.2 M Ammonium sulfate, 0.1 M Sodium acetate trihydrate pH 4.6, 30% PEG MME 2000, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.20 Å R-free 0.244
3K24 Crystal structure of mature apo-Cathepsin L C25A mutant in complex with Gln-Leu-Ala peptide Deposited 2009-09-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 114–333（220 aa） Fragment：mC25A: UNP residues 114-333
Mutation：C138A NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；10% Isopropanol, 0.1 M Sodium acetate trihydrate pH 4.0, 22% PEG 6000, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.50 Å R-free 0.270
3K24 Crystal structure of mature apo-Cathepsin L C25A mutant in complex with Gln-Leu-Ala peptide Deposited 2009-09-29 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Other combination Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 114–333（220 aa） Fragment：mC25A: UNP residues 114-333
Mutation：C138A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；10% Isopropanol, 0.1 M Sodium acetate trihydrate pH 4.0, 22% PEG 6000, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.50 Å R-free 0.270
3KSE Unreduced cathepsin L in complex with stefin A Deposited 2009-11-22 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 114–333（220 aa）
Mutation：T110A,N179D Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；293 K；0.1M Tris-HCl, 16% PEG3000, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 1.71 Å R-free 0.204
3KSE Unreduced cathepsin L in complex with stefin A Deposited 2009-11-22 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 114–333（220 aa）
Mutation：T110A,N179D Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；293 K；0.1M Tris-HCl, 16% PEG3000, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 1.71 Å R-free 0.204
3KSE Unreduced cathepsin L in complex with stefin A Deposited 2009-11-22 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 114–333（220 aa）
Mutation：T110A,N179D Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；293 K；0.1M Tris-HCl, 16% PEG3000, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 1.71 Å R-free 0.204
3OF8 Structural Basis for Reversible and Irreversible Inhibition of Human Cathepsin L by their Respective Dipeptidyl Glyoxal and Diazomethylketone Inhibitors Deposited 2010-08-14 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 113–333（221 aa） Fragment：residues 113-333
Not recorded I0Y Nalpha-[(benzyloxy)carbonyl]-N-[(2S)-1-(4-tert-butoxyphenyl)-4-hydroxy-3-oxobutan-2-yl]-L-phenylalaninamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 5；298 K；20 mM Sodium acetate pH 5.1, 100 mM NaCl, and 1mM EDTA, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.20 Å R-free 0.253
3OF9 Structural Basis for Irreversible Inhibition of Human Cathepsin L by a Diazomethylketone Inhibitor Deposited 2010-08-14 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 113–333（221 aa） Fragment：Cathepsin L
Not recorded I0X Nalpha-[(benzyloxy)carbonyl]-N-[(1S)-1-(4-tert-butoxybenzyl)-3-diazo-2-oxopropyl]-L-phenylalaninamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.2；298 K；30%( w/v) PEG 8K and 200mM Ammonium sulfate, pH 5.2, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
Resolution 1.76 Å R-free 0.249
4AXL HUMAN CATHEPSIN L APO FORM WITH ZN Deposited 2012-06-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 114–333（220 aa） Fragment：CATALYTIC, RESIDUES 114-333
Not recorded ZN ZINC ION × 2 GOL GLYCEROL × 2 ACT ACETATE ION × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.92 Å R-free 0.230
4AXM TRIAZINE CATHEPSIN INHIBITOR COMPLEX Deposited 2012-06-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–333（220 aa） Fragment：CATALYTIC, RESIDUES 114-333
Not recorded GOL GLYCEROL × 1 V65 4-[(4-chlorobenzyl)(cyclohexyl)amino]-6-morpholin-4-yl-1,3,5-triazine-2-carboxamide × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.80 Å R-free 0.257
4AXM TRIAZINE CATHEPSIN INHIBITOR COMPLEX Deposited 2012-06-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 114–333（220 aa） Fragment：CATALYTIC, RESIDUES 114-333
Not recorded GOL GLYCEROL × 1 V65 4-[(4-chlorobenzyl)(cyclohexyl)amino]-6-morpholin-4-yl-1,3,5-triazine-2-carboxamide × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.80 Å R-free 0.257
4AXM TRIAZINE CATHEPSIN INHIBITOR COMPLEX Deposited 2012-06-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain F 114–333（220 aa） Fragment：CATALYTIC, RESIDUES 114-333
Not recorded GOL GLYCEROL × 1 V65 4-[(4-chlorobenzyl)(cyclohexyl)amino]-6-morpholin-4-yl-1,3,5-triazine-2-carboxamide × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.80 Å R-free 0.257
4AXM TRIAZINE CATHEPSIN INHIBITOR COMPLEX Deposited 2012-06-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain I 114–333（220 aa） Fragment：CATALYTIC, RESIDUES 114-333
Not recorded GOL GLYCEROL × 1 V65 4-[(4-chlorobenzyl)(cyclohexyl)amino]-6-morpholin-4-yl-1,3,5-triazine-2-carboxamide × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.80 Å R-free 0.257
4AXM TRIAZINE CATHEPSIN INHIBITOR COMPLEX Deposited 2012-06-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain L 114–333（220 aa） Fragment：CATALYTIC, RESIDUES 114-333
Not recorded GOL GLYCEROL × 1 V65 4-[(4-chlorobenzyl)(cyclohexyl)amino]-6-morpholin-4-yl-1,3,5-triazine-2-carboxamide × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.80 Å R-free 0.257
4AXM TRIAZINE CATHEPSIN INHIBITOR COMPLEX Deposited 2012-06-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 6 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain O 114–333（220 aa） Fragment：CATALYTIC, RESIDUES 114-333
Not recorded GOL GLYCEROL × 1 V65 4-[(4-chlorobenzyl)(cyclohexyl)amino]-6-morpholin-4-yl-1,3,5-triazine-2-carboxamide × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.80 Å R-free 0.257
5F02 CATHEPSIN L IN COMPLEX WITH (2S,4R)-4-(2-Chloro-4-methoxy-benzenesulfonyl)-1-[3-(5-chloro-pyridin-2-yl)-azetidine-3-carbonyl]-pyrrolidine-2-carboxylic acid (1-cyano-cyclopropyl)-amide Deposited 2015-11-27 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–333（220 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 114-333
Not recorded GOL GLYCEROL × 1 5T9 (2~{S},4~{R})-4-[(2-chloranyl-4-methoxy-phenyl)-bis(oxidanyl)-$l^{4}-sulfanyl]-1-[3-(5-chloranylpyridin-2-yl)azetidin-3-yl]carbonyl-~{N}-[1-(iminomethyl)cyclopropyl]pyrrolidine-2-carboxamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；298 K；0.1M MAGNESIUM FORMATE, 15 % PEG 3350
Resolution 1.43 Å R-free 0.191
5I4H Caught in the Act: The Crystal Structure of cleaved Cathepsin L bound to the active site of Cathepsin L Deposited 2016-02-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 113–218（106 aa） Fragment：UNP residues 113-218
Chain B 222–333（112 aa） Fragment：UNP residues 222-333
Mutation：S25C, A110T Mutation：S25C, A110T SO4 SULFATE ION × 4 GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；277 K；0.11 M HEPES, pH 7.5, 2.14 M ammonium sulfate
Resolution 1.42 Å R-free 0.184
5MAE CATHEPSIN L IN COMPLEX WITH (2S,4R)-4-(2-Chloro-4-methoxy-benzenesulfonyl)-1-[3-(5-chloro-pyridin-2-yl)-azetidine-3-carbonyl]-pyrrolidine-2-car boxylic acid (1-cyano-cyclopropyl)-amide Deposited 2016-11-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–333（220 aa） Fragment：UNP residues 114-333
Not recorded 7KN [4-[cyclopentyl(pyrazin-2-ylmethyl)amino]-6-morpholin-4-yl-1,3,5-triazin-2-yl]methylideneazanide × 1 EDO 1,2-ETHANEDIOL × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；295 K；25% PEG3350, 0.1M Bis-Tris
Resolution 1.00 Å R-free 0.182
5MAJ CATHEPSIN L IN COMPLEX WITH 4-[cyclopentyl(imidazo[1,2-a]pyridin-2-ylmethyl)amino]-6-morpholino-1,3,5-triazine-2-carbonitrile Deposited 2016-11-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–333（220 aa）
Not recorded 7KH ~{N}-cyclopentyl-~{N}-(imidazo[1,2-a]pyridin-2-ylmethyl)-4-(iminomethyl)-6-morpholin-4-yl-1,3,5-triazin-2-amine × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；295 K；25% PEG3350, 0.2M ammonium acetate, 0.1M HEPES
Resolution 1.00 Å R-free 0.170
5MQY CATHEPSIN L IN COMPLEX WITH 4-[1,3-benzodioxol-5-ylmethyl(2-phenoxyethyl)amino]-5-fluoropyrimidine-2-carbonitrile Deposited 2016-12-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–333（220 aa）
Not recorded GH4 4-[1,3-benzodioxol-5-ylmethyl(2-phenoxyethyl)amino]-5-fluoropyrimidine-2-carbonitrile × 1 EDO 1,2-ETHANEDIOL × 8 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；294 K；25% PEG3350, 0.1M Bis-Tris
Resolution 1.13 Å R-free 0.199
6EZP CATHEPSIN L IN COMPLEX WITH (3S,14E)-19-chloro-N-(1-cyanocyclopropyl)-5-oxo-12,17-dioxa-4-azatricyclo[16.2.2.06,11]docosa-1(21),6(11),7,9,14,18(22),19-heptaene-3-carboxamide Deposited 2017-11-16 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–333（220 aa）
Not recorded C3E (3~{S},14~{E})-19-chloranyl-~{N}-(1-cyanocyclopropyl)-5-oxidanylidene-12,17-dioxa-4-azatricyclo[16.2.2.0^{6,11}]docosa-1(21),6(11),7,9,14,18(22),19-heptaene-3-carboxamide × 1 GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 3.5；294 K；0.1 M citrate, 25% PEG3350
Resolution 1.37 Å R-free 0.233
6EZX CATHEPSIN L IN COMPLEX WITH (3S,14E)-19-chloro-N-(1-cyanocyclopropyl)-5-oxo-17-oxa-4-azatricyclo[16.2.2.06,11]docosa-1(21),6,8,10,14,18(22),19-heptaene-3-carboxamide Deposited 2017-11-16 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 114–333（220 aa）
Chain B 114–333（220 aa）
Not recorded C7Q (3~{S},14~{E})-19-chloranyl-~{N}-[1-(iminomethyl)cyclopropyl]-5-oxidanylidene-17-oxa-4-azatricyclo[16.2.2.0^{6,11}]docosa-1(21),6,8,10,14,18(22),19-heptaene-3-carboxamide × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；294 K；25% PEG3350, 0.1 M Bis-Tris
Resolution 2.34 Å R-free 0.297
6F06 CATHEPSIN L IN COMPLEX WITH (3S,14E)-8-(azetidin-3-yl)-19-chloro-N-(1-cyanocyclopropyl)-5-oxo-12,17-dioxa-4-azatricyclo[16.2.2.06,11]docosa-1(21),6,8,10,14,18(22),19-heptaene-3-carboxamide Deposited 2017-11-17 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–333（220 aa）
Not recorded C7T (3~{S},14~{E})-8-(azetidin-3-yl)-19-chloranyl-~{N}-(1-cyanocyclopropyl)-5-oxidanylidene-12,17-dioxa-4-azatricyclo[16.2.2.0^{6,11}]docosa-1(21),6(11),7,9,14,18(22),19-heptaene-3-carboxamide × 1 ZN ZINC ION × 6 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；294 K；20% PEG3350, 0.05 M zinc acetate
Resolution 2.02 Å R-free 0.274
6F06 CATHEPSIN L IN COMPLEX WITH (3S,14E)-8-(azetidin-3-yl)-19-chloro-N-(1-cyanocyclopropyl)-5-oxo-12,17-dioxa-4-azatricyclo[16.2.2.06,11]docosa-1(21),6,8,10,14,18(22),19-heptaene-3-carboxamide Deposited 2017-11-17 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 114–333（220 aa）
Not recorded C7T (3~{S},14~{E})-8-(azetidin-3-yl)-19-chloranyl-~{N}-(1-cyanocyclopropyl)-5-oxidanylidene-12,17-dioxa-4-azatricyclo[16.2.2.0^{6,11}]docosa-1(21),6(11),7,9,14,18(22),19-heptaene-3-carboxamide × 1 ZN ZINC ION × 8 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；294 K；20% PEG3350, 0.05 M zinc acetate
Resolution 2.02 Å R-free 0.274
6JD0 Structure of mutant human cathepsin L, engineered for GAG binding Deposited 2019-01-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 18–333（316 aa）
Mutation：E105K, C121S, L165Y, M257L, G260A, M291N, G292K, A310L GOL GLYCEROL × 14 CL CHLORIDE ION × 3 NA SODIUM ION × 5 PO4 PHOSPHATE ION × 8 POL N-PROPANOL × 10 PGE TRIETHYLENE GLYCOL × 6 EOH ETHANOL × 3 EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；293 K；PEG 4000, 2-propanol etc
Resolution 1.80 Å R-free 0.215
6JD8 Structure of a proline specific mutant of human cathepsin L Deposited 2019-01-31 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 18–333（316 aa）
Mutation：C138S,L182Y,M274L,G277A,A327L GOL GLYCEROL × 1 EOH ETHANOL × 12 PEG DI(HYDROXYETHYL)ETHER × 1 EDO 1,2-ETHANEDIOL × 1 PGE TRIETHYLENE GLYCOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；293 K；PEG 4000, 2-propanol
Resolution 1.46 Å R-free 0.237
7QKB Crystal structure of human Cathepsin L in complex with covalently bound GC376 Deposited 2021-12-17 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–333（220 aa）
Mutation：T110A PEG DI(HYDROXYETHYL)ETHER × 2 NA SODIUM ION × 1 PGE TRIETHYLENE GLYCOL × 1 CL CHLORIDE ION × 1 UED N~2~-[(benzyloxy)carbonyl]-N-{(2S)-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}-L-leucinamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.80 Å R-free 0.203
7QKB Crystal structure of human Cathepsin L in complex with covalently bound GC376 Deposited 2021-12-17 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 114–333（220 aa）
Mutation：T110A PEG DI(HYDROXYETHYL)ETHER × 3 NA SODIUM ION × 1 PGE TRIETHYLENE GLYCOL × 1 UED N~2~-[(benzyloxy)carbonyl]-N-{(2S)-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}-L-leucinamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.80 Å R-free 0.203
7QKB Crystal structure of human Cathepsin L in complex with covalently bound GC376 Deposited 2021-12-17 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 114–333（220 aa）
Mutation：T110A PEG DI(HYDROXYETHYL)ETHER × 2 NA SODIUM ION × 1 UED N~2~-[(benzyloxy)carbonyl]-N-{(2S)-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}-L-leucinamide × 1 PG4 TETRAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.80 Å R-free 0.203
7QKB Crystal structure of human Cathepsin L in complex with covalently bound GC376 Deposited 2021-12-17 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 114–333（220 aa）
Mutation：T110A NA SODIUM ION × 1 UED N~2~-[(benzyloxy)carbonyl]-N-{(2S)-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}-L-leucinamide × 1 P6G HEXAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.80 Å R-free 0.203
7QKC Crystal structure of human Cathepsin L after incubation with Sulfo-Calpeptin Deposited 2021-12-17 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–333（220 aa）
Mutation：T110A PEG DI(HYDROXYETHYL)ETHER × 2 RN2 Calpeptin × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.69 Å R-free 0.179
7QKC Crystal structure of human Cathepsin L after incubation with Sulfo-Calpeptin Deposited 2021-12-17 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 114–333（220 aa）
Mutation：T110A PEG DI(HYDROXYETHYL)ETHER × 1 RN2 Calpeptin × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.69 Å R-free 0.179
7QKC Crystal structure of human Cathepsin L after incubation with Sulfo-Calpeptin Deposited 2021-12-17 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 114–333（220 aa）
Mutation：T110A PEG DI(HYDROXYETHYL)ETHER × 3 RN2 Calpeptin × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.69 Å R-free 0.179
7QKC Crystal structure of human Cathepsin L after incubation with Sulfo-Calpeptin Deposited 2021-12-17 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 114–333（220 aa）
Mutation：T110A PEG DI(HYDROXYETHYL)ETHER × 1 RN2 Calpeptin × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.69 Å R-free 0.179
7QKD Crystal structure of human Cathepsin L in complex with covalently bound MG132 Deposited 2021-12-17 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–333（220 aa）
Mutation：T110A ALD N-[(benzyloxy)carbonyl]-L-leucyl-N-[(2S)-1-hydroxy-4-methylpentan-2-yl]-L-leucinamide × 1 PEG DI(HYDROXYETHYL)ETHER × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.50 Å R-free 0.198
7QKD Crystal structure of human Cathepsin L in complex with covalently bound MG132 Deposited 2021-12-17 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 114–333（220 aa）
Mutation：T110A ALD N-[(benzyloxy)carbonyl]-L-leucyl-N-[(2S)-1-hydroxy-4-methylpentan-2-yl]-L-leucinamide × 1 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.50 Å R-free 0.198
7QKD Crystal structure of human Cathepsin L in complex with covalently bound MG132 Deposited 2021-12-17 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 114–333（220 aa）
Mutation：T110A ALD N-[(benzyloxy)carbonyl]-L-leucyl-N-[(2S)-1-hydroxy-4-methylpentan-2-yl]-L-leucinamide × 1 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.50 Å R-free 0.198
7QKD Crystal structure of human Cathepsin L in complex with covalently bound MG132 Deposited 2021-12-17 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 114–333（220 aa）
Mutation：T110A ALD N-[(benzyloxy)carbonyl]-L-leucyl-N-[(2S)-1-hydroxy-4-methylpentan-2-yl]-L-leucinamide × 1 PEG DI(HYDROXYETHYL)ETHER × 3 ACT ACETATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.50 Å R-free 0.198
7W33 The crystal structure of human CtsL in complex with 14a Deposited 2021-11-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–333（333 aa）
Not recorded 89B N-[(2S)-3-(4-fluorophenyl)-1-oxidanylidene-1-[[(2R,3S)-3-oxidanyl-4-oxidanylidene-1-[(3S)-2-oxidanylidenepiperidin-3-yl]-4-[(phenylmethyl)amino]butan-2-yl]amino]propan-2-yl]-1-benzofuran-2-carboxamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.1；289.15 K；100mM sodium acetate (pH 4.1), 15% (w/v) PEG 2000, protein concentration 8 mg/ml
Resolution 2.39 Å R-free 0.261
7W34 The crystal structure of human CtsL in complex with 14b Deposited 2021-11-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–333（333 aa）
Not recorded 89K N-[(2S)-3-cyclohexyl-1-oxidanylidene-1-[[(2S,3S)-3-oxidanyl-4-oxidanylidene-1-[(3S)-2-oxidanylidenepiperidin-3-yl]-4-[(phenylmethyl)amino]butan-2-yl]amino]propan-2-yl]-1-benzofuran-2-carboxamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.1；289.15 K；100mM sodium acetate (pH 4.1), 15% (w/v) PEG 2000, protein concentration 8mg/ml
Resolution 2.89 Å R-free 0.303
7Z3T Crystal structure of apo human Cathepsin L Deposited 2022-03-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–333（220 aa）
Mutation：T110A Non-standard monomer：Yes (specific site not provided by mmCIF) PEG DI(HYDROXYETHYL)ETHER × 3 PGE TRIETHYLENE GLYCOL × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days.
Resolution 1.60 Å R-free 0.176
7Z3T Crystal structure of apo human Cathepsin L Deposited 2022-03-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 114–333（220 aa）
Mutation：T110A Non-standard monomer：Yes (specific site not provided by mmCIF) PEG DI(HYDROXYETHYL)ETHER × 2 PGE TRIETHYLENE GLYCOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days.
Resolution 1.60 Å R-free 0.176
7Z3T Crystal structure of apo human Cathepsin L Deposited 2022-03-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 114–333（220 aa）
Mutation：T110A Non-standard monomer：Yes (specific site not provided by mmCIF) PEG DI(HYDROXYETHYL)ETHER × 3 EDO 1,2-ETHANEDIOL × 1 1PE PENTAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days.
Resolution 1.60 Å R-free 0.176
7Z3T Crystal structure of apo human Cathepsin L Deposited 2022-03-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 114–333（220 aa）
Mutation：T110A Non-standard monomer：Yes (specific site not provided by mmCIF) PGE TRIETHYLENE GLYCOL × 1 EDO 1,2-ETHANEDIOL × 1 1PE PENTAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days.
Resolution 1.60 Å R-free 0.176
7Z58 Crystal structure of human Cathepsin L in complex with covalently bound Calpeptin Deposited 2022-03-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–333（220 aa）
Mutation：T110A PEG DI(HYDROXYETHYL)ETHER × 2 PGE TRIETHYLENE GLYCOL × 2 EDO 1,2-ETHANEDIOL × 1 RN2 Calpeptin × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.35 Å R-free 0.158
7Z58 Crystal structure of human Cathepsin L in complex with covalently bound Calpeptin Deposited 2022-03-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 114–333（220 aa）
Mutation：T110A PEG DI(HYDROXYETHYL)ETHER × 2 EDO 1,2-ETHANEDIOL × 1 RN2 Calpeptin × 1 DMS DIMETHYL SULFOXIDE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.35 Å R-free 0.158
7Z58 Crystal structure of human Cathepsin L in complex with covalently bound Calpeptin Deposited 2022-03-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 114–333（220 aa）
Mutation：T110A PEG DI(HYDROXYETHYL)ETHER × 2 PGE TRIETHYLENE GLYCOL × 1 EDO 1,2-ETHANEDIOL × 1 RN2 Calpeptin × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.35 Å R-free 0.158
7Z58 Crystal structure of human Cathepsin L in complex with covalently bound Calpeptin Deposited 2022-03-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 114–333（220 aa）
Mutation：T110A PEG DI(HYDROXYETHYL)ETHER × 2 PGE TRIETHYLENE GLYCOL × 2 RN2 Calpeptin × 1 DMS DIMETHYL SULFOXIDE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.35 Å R-free 0.158
7ZS7 Crystal structure of human cathepsin L with covalently bound calpain inhibitor VI Deposited 2022-05-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–333（220 aa）
Mutation：T110A JQO (2S)-2-[(4-fluorophenyl)sulfonylamino]-3-methyl-N-[(2S)-4-methyl-1-oxidanyl-pentan-2-yl]butanamide × 1 DMS DIMETHYL SULFOXIDE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.60 Å R-free 0.188
7ZS7 Crystal structure of human cathepsin L with covalently bound calpain inhibitor VI Deposited 2022-05-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 114–333（220 aa）
Mutation：T110A JQO (2S)-2-[(4-fluorophenyl)sulfonylamino]-3-methyl-N-[(2S)-4-methyl-1-oxidanyl-pentan-2-yl]butanamide × 1 DMS DIMETHYL SULFOXIDE × 2 ACT ACETATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.60 Å R-free 0.188
7ZS7 Crystal structure of human cathepsin L with covalently bound calpain inhibitor VI Deposited 2022-05-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 114–333（220 aa）
Mutation：T110A JQO (2S)-2-[(4-fluorophenyl)sulfonylamino]-3-methyl-N-[(2S)-4-methyl-1-oxidanyl-pentan-2-yl]butanamide × 1 DMS DIMETHYL SULFOXIDE × 1 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.60 Å R-free 0.188
7ZS7 Crystal structure of human cathepsin L with covalently bound calpain inhibitor VI Deposited 2022-05-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 114–333（220 aa）
Mutation：T110A JQO (2S)-2-[(4-fluorophenyl)sulfonylamino]-3-methyl-N-[(2S)-4-methyl-1-oxidanyl-pentan-2-yl]butanamide × 1 DMS DIMETHYL SULFOXIDE × 4 PEG DI(HYDROXYETHYL)ETHER × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.60 Å R-free 0.188
7ZVF Crystal structure of human cathepsin L in complex with covalently bound CLIK148 Deposited 2022-05-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–333（220 aa）
Mutation：T110A KXL (2S)-N-[(2S)-1-(dimethylamino)-1-oxidanylidene-3-phenyl-propan-2-yl]-2-oxidanyl-N'-(2-pyridin-2-ylethyl)butanediamide × 1 PG4 TETRAETHYLENE GLYCOL × 1 1PE PENTAETHYLENE GLYCOL × 1 DMS DIMETHYL SULFOXIDE × 2 PEG DI(HYDROXYETHYL)ETHER × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.60 Å R-free 0.189
7ZVF Crystal structure of human cathepsin L in complex with covalently bound CLIK148 Deposited 2022-05-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 114–333（220 aa）
Mutation：T110A KXL (2S)-N-[(2S)-1-(dimethylamino)-1-oxidanylidene-3-phenyl-propan-2-yl]-2-oxidanyl-N'-(2-pyridin-2-ylethyl)butanediamide × 1 1PE PENTAETHYLENE GLYCOL × 1 DMS DIMETHYL SULFOXIDE × 2 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.60 Å R-free 0.189
7ZVF Crystal structure of human cathepsin L in complex with covalently bound CLIK148 Deposited 2022-05-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 114–333（220 aa）
Mutation：T110A KXL (2S)-N-[(2S)-1-(dimethylamino)-1-oxidanylidene-3-phenyl-propan-2-yl]-2-oxidanyl-N'-(2-pyridin-2-ylethyl)butanediamide × 1 1PE PENTAETHYLENE GLYCOL × 1 PEG DI(HYDROXYETHYL)ETHER × 1 NA SODIUM ION × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.60 Å R-free 0.189
7ZVF Crystal structure of human cathepsin L in complex with covalently bound CLIK148 Deposited 2022-05-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 114–333（220 aa）
Mutation：T110A KXL (2S)-N-[(2S)-1-(dimethylamino)-1-oxidanylidene-3-phenyl-propan-2-yl]-2-oxidanyl-N'-(2-pyridin-2-ylethyl)butanediamide × 1 1PE PENTAETHYLENE GLYCOL × 1 DMS DIMETHYL SULFOXIDE × 3 PEG DI(HYDROXYETHYL)ETHER × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.60 Å R-free 0.189
7ZXA Crystal structure of human cathepsin L with covalently bound aloxistatin (E-64D) Deposited 2022-05-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–333（220 aa）
Mutation：T110A E6D ethyl (3S)-3-hydroxy-4-({(2S)-4-methyl-1-[(3-methylbutyl)amino]-1-oxopentan-2-yl}amino)-4-oxobutanoate × 1 1PE PENTAETHYLENE GLYCOL × 1 PG4 TETRAETHYLENE GLYCOL × 1 DMS DIMETHYL SULFOXIDE × 1 PEG DI(HYDROXYETHYL)ETHER × 1 PGE TRIETHYLENE GLYCOL × 2 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.60 Å R-free 0.194
7ZXA Crystal structure of human cathepsin L with covalently bound aloxistatin (E-64D) Deposited 2022-05-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 114–333（220 aa）
Mutation：T110A E6D ethyl (3S)-3-hydroxy-4-({(2S)-4-methyl-1-[(3-methylbutyl)amino]-1-oxopentan-2-yl}amino)-4-oxobutanoate × 1 DMS DIMETHYL SULFOXIDE × 2 PEG DI(HYDROXYETHYL)ETHER × 3 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.60 Å R-free 0.194
7ZXA Crystal structure of human cathepsin L with covalently bound aloxistatin (E-64D) Deposited 2022-05-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 114–333（220 aa）
Mutation：T110A E6D ethyl (3S)-3-hydroxy-4-({(2S)-4-methyl-1-[(3-methylbutyl)amino]-1-oxopentan-2-yl}amino)-4-oxobutanoate × 1 PEG DI(HYDROXYETHYL)ETHER × 3 PGE TRIETHYLENE GLYCOL × 1 EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.60 Å R-free 0.194
7ZXA Crystal structure of human cathepsin L with covalently bound aloxistatin (E-64D) Deposited 2022-05-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 114–333（220 aa）
Mutation：T110A E6D ethyl (3S)-3-hydroxy-4-({(2S)-4-methyl-1-[(3-methylbutyl)amino]-1-oxopentan-2-yl}amino)-4-oxobutanoate × 1 PG4 TETRAETHYLENE GLYCOL × 1 DMS DIMETHYL SULFOXIDE × 2 PEG DI(HYDROXYETHYL)ETHER × 1 PGE TRIETHYLENE GLYCOL × 1 EDO 1,2-ETHANEDIOL × 1 P6G HEXAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.60 Å R-free 0.194
8A4U Crystal structure of human cathepsin L with CAA0225 Deposited 2022-06-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–333（220 aa）
Mutation：T110A Non-standard monomer：Yes (specific site not provided by mmCIF) L2X (2S,3S)-N3-[2-(4-hydroxyphenyl)ethyl]-N2-[(2S)-1-oxidanylidene-3-phenyl-1-[(phenylmethyl)amino]propan-2-yl]oxirane-2,3-dicarboxamide × 1 NA SODIUM ION × 2 PEG DI(HYDROXYETHYL)ETHER × 5 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.90 Å R-free 0.209
8A4U Crystal structure of human cathepsin L with CAA0225 Deposited 2022-06-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 114–333（220 aa）
Mutation：T110A Non-standard monomer：Yes (specific site not provided by mmCIF) L2X (2S,3S)-N3-[2-(4-hydroxyphenyl)ethyl]-N2-[(2S)-1-oxidanylidene-3-phenyl-1-[(phenylmethyl)amino]propan-2-yl]oxirane-2,3-dicarboxamide × 1 PEG DI(HYDROXYETHYL)ETHER × 1 PGE TRIETHYLENE GLYCOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.90 Å R-free 0.209
8A4U Crystal structure of human cathepsin L with CAA0225 Deposited 2022-06-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 114–333（220 aa）
Mutation：T110A Non-standard monomer：Yes (specific site not provided by mmCIF) L2X (2S,3S)-N3-[2-(4-hydroxyphenyl)ethyl]-N2-[(2S)-1-oxidanylidene-3-phenyl-1-[(phenylmethyl)amino]propan-2-yl]oxirane-2,3-dicarboxamide × 1 NA SODIUM ION × 1 PEG DI(HYDROXYETHYL)ETHER × 2 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.90 Å R-free 0.209
8A4U Crystal structure of human cathepsin L with CAA0225 Deposited 2022-06-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 114–333（220 aa）
Mutation：T110A Non-standard monomer：Yes (specific site not provided by mmCIF) L2X (2S,3S)-N3-[2-(4-hydroxyphenyl)ethyl]-N2-[(2S)-1-oxidanylidene-3-phenyl-1-[(phenylmethyl)amino]propan-2-yl]oxirane-2,3-dicarboxamide × 1 PEG DI(HYDROXYETHYL)ETHER × 1 EDO 1,2-ETHANEDIOL × 1 PG4 TETRAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.90 Å R-free 0.209
8A4V Crystal structure of human cathepsin L with covalently bound E-64 Deposited 2022-06-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–333（220 aa）
Mutation：T110A E64 N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE × 1 PEG DI(HYDROXYETHYL)ETHER × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.65 Å R-free 0.203
8A4V Crystal structure of human cathepsin L with covalently bound E-64 Deposited 2022-06-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 114–333（220 aa）
Mutation：T110A E64 N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE × 1 PEG DI(HYDROXYETHYL)ETHER × 1 DMS DIMETHYL SULFOXIDE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.65 Å R-free 0.203
8A4V Crystal structure of human cathepsin L with covalently bound E-64 Deposited 2022-06-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 114–333（220 aa）
Mutation：T110A E64 N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE × 1 PEG DI(HYDROXYETHYL)ETHER × 1 PGE TRIETHYLENE GLYCOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.65 Å R-free 0.203
8A4V Crystal structure of human cathepsin L with covalently bound E-64 Deposited 2022-06-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 114–333（220 aa）
Mutation：T110A E64 N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE × 1 PEG DI(HYDROXYETHYL)ETHER × 1 DMS DIMETHYL SULFOXIDE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.65 Å R-free 0.203
8A4W Crystal structure of human cathepsin L with covalently bound Cathepsin L inhibitor IV Deposited 2022-06-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–333（220 aa）
Mutation：T110A L2F N-(1-naphthylsulfonyl)-(L)-isoleucyl-(L)-tryptophanol × 1 PEG DI(HYDROXYETHYL)ETHER × 1 EDO 1,2-ETHANEDIOL × 1 DMS DIMETHYL SULFOXIDE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.40 Å R-free 0.167
8A4W Crystal structure of human cathepsin L with covalently bound Cathepsin L inhibitor IV Deposited 2022-06-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 114–333（220 aa）
Mutation：T110A L2F N-(1-naphthylsulfonyl)-(L)-isoleucyl-(L)-tryptophanol × 1 EDO 1,2-ETHANEDIOL × 1 DMS DIMETHYL SULFOXIDE × 3 PG4 TETRAETHYLENE GLYCOL × 1 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.40 Å R-free 0.167
8A4W Crystal structure of human cathepsin L with covalently bound Cathepsin L inhibitor IV Deposited 2022-06-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 114–333（220 aa）
Mutation：T110A L2F N-(1-naphthylsulfonyl)-(L)-isoleucyl-(L)-tryptophanol × 1 DMS DIMETHYL SULFOXIDE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.40 Å R-free 0.167
8A4W Crystal structure of human cathepsin L with covalently bound Cathepsin L inhibitor IV Deposited 2022-06-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 114–333（220 aa）
Mutation：T110A L2F N-(1-naphthylsulfonyl)-(L)-isoleucyl-(L)-tryptophanol × 1 PEG DI(HYDROXYETHYL)ETHER × 2 DMS DIMETHYL SULFOXIDE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.40 Å R-free 0.167
8A4X Crystal structure of human Cathepsin L with covalently bound Calpain inhibitor III Deposited 2022-06-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–333（220 aa）
Mutation：T110A L3F (phenylmethyl) N-[(2S)-3-methyl-1-oxidanylidene-1-[[(2S)-1-oxidanyl-3-phenyl-propan-2-yl]amino]butan-2-yl]carbamate × 1 PEG DI(HYDROXYETHYL)ETHER × 1 PGE TRIETHYLENE GLYCOL × 1 PG4 TETRAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.80 Å R-free 0.226
8A4X Crystal structure of human Cathepsin L with covalently bound Calpain inhibitor III Deposited 2022-06-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 114–333（220 aa）
Mutation：T110A L3F (phenylmethyl) N-[(2S)-3-methyl-1-oxidanylidene-1-[[(2S)-1-oxidanyl-3-phenyl-propan-2-yl]amino]butan-2-yl]carbamate × 1 PEG DI(HYDROXYETHYL)ETHER × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.80 Å R-free 0.226
8A4X Crystal structure of human Cathepsin L with covalently bound Calpain inhibitor III Deposited 2022-06-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 114–333（220 aa）
Mutation：T110A L3F (phenylmethyl) N-[(2S)-3-methyl-1-oxidanylidene-1-[[(2S)-1-oxidanyl-3-phenyl-propan-2-yl]amino]butan-2-yl]carbamate × 1 PEG DI(HYDROXYETHYL)ETHER × 2 P6G HEXAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.80 Å R-free 0.226
8A4X Crystal structure of human Cathepsin L with covalently bound Calpain inhibitor III Deposited 2022-06-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 114–333（220 aa）
Mutation：T110A L3F (phenylmethyl) N-[(2S)-3-methyl-1-oxidanylidene-1-[[(2S)-1-oxidanyl-3-phenyl-propan-2-yl]amino]butan-2-yl]carbamate × 1 P6G HEXAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.80 Å R-free 0.226
8A5B Crystal structure of human cathepsin L in complex with covalently bound MG-101 Deposited 2022-06-14 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 114–333（220 aa）
Mutation：T110A PGE TRIETHYLENE GLYCOL × 1 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.80 Å R-free 0.225
8A5B Crystal structure of human cathepsin L in complex with covalently bound MG-101 Deposited 2022-06-14 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 114–333（220 aa）
Mutation：T110A NA SODIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.80 Å R-free 0.225
8A5B Crystal structure of human cathepsin L in complex with covalently bound MG-101 Deposited 2022-06-14 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 114–333（220 aa）
Mutation：T110A PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.80 Å R-free 0.225
8A5B Crystal structure of human cathepsin L in complex with covalently bound MG-101 Deposited 2022-06-14 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 114–333（220 aa）
Mutation：T110A NA SODIUM ION × 1 PEG DI(HYDROXYETHYL)ETHER × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.80 Å R-free 0.225
8AHV Crystal structure of human cathepsin L in complex with calpain inhibitor XII Deposited 2022-07-22 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–333（220 aa）
Mutation：T110A PGE TRIETHYLENE GLYCOL × 2 M6L (phenylmethyl) ~{N}-[(2~{S})-4-methyl-1-oxidanylidene-1-[[(2~{S},3~{S})-2-oxidanyl-1-oxidanylidene-1-(pyridin-2-ylmethylamino)hexan-3-yl]amino]pentan-2-yl]carbamate × 1 DMS DIMETHYL SULFOXIDE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.70 Å R-free 0.207
8AHV Crystal structure of human cathepsin L in complex with calpain inhibitor XII Deposited 2022-07-22 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 114–333（220 aa）
Mutation：T110A M6L (phenylmethyl) ~{N}-[(2~{S})-4-methyl-1-oxidanylidene-1-[[(2~{S},3~{S})-2-oxidanyl-1-oxidanylidene-1-(pyridin-2-ylmethylamino)hexan-3-yl]amino]pentan-2-yl]carbamate × 1 EDO 1,2-ETHANEDIOL × 2 PEG DI(HYDROXYETHYL)ETHER × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.70 Å R-free 0.207
8AHV Crystal structure of human cathepsin L in complex with calpain inhibitor XII Deposited 2022-07-22 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 114–333（220 aa）
Mutation：T110A M6L (phenylmethyl) ~{N}-[(2~{S})-4-methyl-1-oxidanylidene-1-[[(2~{S},3~{S})-2-oxidanyl-1-oxidanylidene-1-(pyridin-2-ylmethylamino)hexan-3-yl]amino]pentan-2-yl]carbamate × 1 DMS DIMETHYL SULFOXIDE × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.70 Å R-free 0.207
8AHV Crystal structure of human cathepsin L in complex with calpain inhibitor XII Deposited 2022-07-22 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 114–333（220 aa）
Mutation：T110A M6L (phenylmethyl) ~{N}-[(2~{S})-4-methyl-1-oxidanylidene-1-[[(2~{S},3~{S})-2-oxidanyl-1-oxidanylidene-1-(pyridin-2-ylmethylamino)hexan-3-yl]amino]pentan-2-yl]carbamate × 1 DMS DIMETHYL SULFOXIDE × 2 EDO 1,2-ETHANEDIOL × 1 PEG DI(HYDROXYETHYL)ETHER × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.70 Å R-free 0.207
8B4F Crystal structure of human cathepsin L forming a thiohemiacetal with N-Boc-2-aminoacetaldehyde Deposited 2022-09-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–333（220 aa）
Mutation：T110A OYU ~{tert}-butyl ~{N}-(2-hydroxyethyl)carbamate × 1 PGE TRIETHYLENE GLYCOL × 1 DMS DIMETHYL SULFOXIDE × 1 EDO 1,2-ETHANEDIOL × 2 PEG DI(HYDROXYETHYL)ETHER × 1 NA SODIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.90 Å R-free 0.210
8B4F Crystal structure of human cathepsin L forming a thiohemiacetal with N-Boc-2-aminoacetaldehyde Deposited 2022-09-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 114–333（220 aa）
Mutation：T110A OYU ~{tert}-butyl ~{N}-(2-hydroxyethyl)carbamate × 1 EDO 1,2-ETHANEDIOL × 2 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.90 Å R-free 0.210
8B4F Crystal structure of human cathepsin L forming a thiohemiacetal with N-Boc-2-aminoacetaldehyde Deposited 2022-09-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 114–333（220 aa）
Mutation：T110A OYU ~{tert}-butyl ~{N}-(2-hydroxyethyl)carbamate × 1 EDO 1,2-ETHANEDIOL × 2 PEG DI(HYDROXYETHYL)ETHER × 2 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.90 Å R-free 0.210
8B4F Crystal structure of human cathepsin L forming a thiohemiacetal with N-Boc-2-aminoacetaldehyde Deposited 2022-09-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 114–333（220 aa）
Mutation：T110A OYU ~{tert}-butyl ~{N}-(2-hydroxyethyl)carbamate × 1 DMS DIMETHYL SULFOXIDE × 2 EDO 1,2-ETHANEDIOL × 2 PEG DI(HYDROXYETHYL)ETHER × 5 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.90 Å R-free 0.210
8B4F Crystal structure of human cathepsin L forming a thiohemiacetal with N-Boc-2-aminoacetaldehyde Deposited 2022-09-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 5 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 114–333（220 aa）
Chain B 114–333（220 aa）
Chain C 114–333（220 aa）
Chain D 114–333（220 aa）
Mutation：T110A Mutation：T110A Mutation：T110A Mutation：T110A OYU ~{tert}-butyl ~{N}-(2-hydroxyethyl)carbamate × 4 PGE TRIETHYLENE GLYCOL × 1 DMS DIMETHYL SULFOXIDE × 3 EDO 1,2-ETHANEDIOL × 8 PEG DI(HYDROXYETHYL)ETHER × 9 NA SODIUM ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.90 Å R-free 0.210
8C77 Human cathepsin L after reaction with the thiocarbazate inhibitor CID 16725315 Deposited 2023-01-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–333（220 aa）
Mutation：T110A TXH ~{tert}-butyl ~{N}-[(2~{S})-3-(1~{H}-indol-3-yl)-1-(2-methanoylhydrazinyl)-1-oxidanylidene-propan-2-yl]carbamate × 1 EDO 1,2-ETHANEDIOL × 4 PG4 TETRAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.70 Å R-free 0.197
8C77 Human cathepsin L after reaction with the thiocarbazate inhibitor CID 16725315 Deposited 2023-01-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 114–333（220 aa）
Mutation：T110A TXH ~{tert}-butyl ~{N}-[(2~{S})-3-(1~{H}-indol-3-yl)-1-(2-methanoylhydrazinyl)-1-oxidanylidene-propan-2-yl]carbamate × 1 EDO 1,2-ETHANEDIOL × 1 PG4 TETRAETHYLENE GLYCOL × 1 DMS DIMETHYL SULFOXIDE × 4 PEG DI(HYDROXYETHYL)ETHER × 1 ACT ACETATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.70 Å R-free 0.197
8C77 Human cathepsin L after reaction with the thiocarbazate inhibitor CID 16725315 Deposited 2023-01-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 114–333（220 aa）
Mutation：T110A TXH ~{tert}-butyl ~{N}-[(2~{S})-3-(1~{H}-indol-3-yl)-1-(2-methanoylhydrazinyl)-1-oxidanylidene-propan-2-yl]carbamate × 1 EDO 1,2-ETHANEDIOL × 2 PG4 TETRAETHYLENE GLYCOL × 1 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.70 Å R-free 0.197
8C77 Human cathepsin L after reaction with the thiocarbazate inhibitor CID 16725315 Deposited 2023-01-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 114–333（220 aa）
Mutation：T110A TXH ~{tert}-butyl ~{N}-[(2~{S})-3-(1~{H}-indol-3-yl)-1-(2-methanoylhydrazinyl)-1-oxidanylidene-propan-2-yl]carbamate × 1 EDO 1,2-ETHANEDIOL × 1 PG4 TETRAETHYLENE GLYCOL × 2 PEG DI(HYDROXYETHYL)ETHER × 1 PGE TRIETHYLENE GLYCOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.70 Å R-free 0.197
8GX2 The crystal structure of human CtsL in complex with 14c Deposited 2022-09-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–333（333 aa）
Not recorded DMS DIMETHYL SULFOXIDE × 2 KJ0 N-[(2S)-3-cyclohexyl-1-[[(2S,3S)-4-(cyclopropylamino)-3-oxidanyl-4-oxidanylidene-1-[(3S)-2-oxidanylidenepiperidin-3-yl]butan-2-yl]amino]-1-oxidanylidene-propan-2-yl]-1-benzofuran-2-carboxamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；289.15 K；100mM sodium acetate (pH 4.1), 15% (w/v) PEG 2000, 8mg/ml protein
Resolution 2.00 Å R-free 0.232
8GX2 The crystal structure of human CtsL in complex with 14c Deposited 2022-09-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 1–333（333 aa）
Not recorded DMS DIMETHYL SULFOXIDE × 1 KJ0 N-[(2S)-3-cyclohexyl-1-[[(2S,3S)-4-(cyclopropylamino)-3-oxidanyl-4-oxidanylidene-1-[(3S)-2-oxidanylidenepiperidin-3-yl]butan-2-yl]amino]-1-oxidanylidene-propan-2-yl]-1-benzofuran-2-carboxamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；289.15 K；100mM sodium acetate (pH 4.1), 15% (w/v) PEG 2000, 8mg/ml protein
Resolution 2.00 Å R-free 0.232
8HET Crystal structure of CTSL in complex with E64d Deposited 2022-11-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–333（220 aa）
Not recorded E6D ethyl (3S)-3-hydroxy-4-({(2S)-4-methyl-1-[(3-methylbutyl)amino]-1-oxopentan-2-yl}amino)-4-oxobutanoate × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；100mM Citric acid, 3M Sodium chloride, pH 3.5
Resolution 2.00 Å R-free 0.213
8HFV Crystal structure of CTSL in complex with K777 Deposited 2022-11-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–333（220 aa）
Not recorded ZN ZINC ION × 7 CAC CACODYLATE ION × 2 0IW Nalpha-[(4-methylpiperazin-1-yl)carbonyl]-N-[(3S)-1-phenyl-5-(phenylsulfonyl)pentan-3-yl]-L-phenylalaninamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；9% (v/v) 2-propanol, 90mM Sodium cacodylate/ Hydrochloric acid pH 6.5, 180mM Zinc acetate, 0.5% w/v n-dodecyl-N,N-dimethylamine-N-oxide
Resolution 2.10 Å R-free 0.242
8HFV Crystal structure of CTSL in complex with K777 Deposited 2022-11-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 114–333（220 aa）
Not recorded ZN ZINC ION × 7 CAC CACODYLATE ION × 2 0IW Nalpha-[(4-methylpiperazin-1-yl)carbonyl]-N-[(3S)-1-phenyl-5-(phenylsulfonyl)pentan-3-yl]-L-phenylalaninamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；9% (v/v) 2-propanol, 90mM Sodium cacodylate/ Hydrochloric acid pH 6.5, 180mM Zinc acetate, 0.5% w/v n-dodecyl-N,N-dimethylamine-N-oxide
Resolution 2.10 Å R-free 0.242
8HFV Crystal structure of CTSL in complex with K777 Deposited 2022-11-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 114–333（220 aa）
Not recorded ZN ZINC ION × 7 CAC CACODYLATE ION × 2 0IW Nalpha-[(4-methylpiperazin-1-yl)carbonyl]-N-[(3S)-1-phenyl-5-(phenylsulfonyl)pentan-3-yl]-L-phenylalaninamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；9% (v/v) 2-propanol, 90mM Sodium cacodylate/ Hydrochloric acid pH 6.5, 180mM Zinc acetate, 0.5% w/v n-dodecyl-N,N-dimethylamine-N-oxide
Resolution 2.10 Å R-free 0.242
8HFV Crystal structure of CTSL in complex with K777 Deposited 2022-11-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 114–333（220 aa）
Not recorded ZN ZINC ION × 7 CAC CACODYLATE ION × 2 0IW Nalpha-[(4-methylpiperazin-1-yl)carbonyl]-N-[(3S)-1-phenyl-5-(phenylsulfonyl)pentan-3-yl]-L-phenylalaninamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；9% (v/v) 2-propanol, 90mM Sodium cacodylate/ Hydrochloric acid pH 6.5, 180mM Zinc acetate, 0.5% w/v n-dodecyl-N,N-dimethylamine-N-oxide
Resolution 2.10 Å R-free 0.242
8OFA Crystal structure of human cathepsin L interacting with tosyl phenylalanyl chloromethyl ketone (TPCK) Deposited 2023-03-14 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–333（220 aa）
Mutation：T110A TQ8 N-[(2S)-4-chloro-3-oxo-1-phenyl-butan-2-yl]-4-methyl-benzenesulfonamide × 1 EDO 1,2-ETHANEDIOL × 1 PEG DI(HYDROXYETHYL)ETHER × 2 DMS DIMETHYL SULFOXIDE × 3 PGE TRIETHYLENE GLYCOL × 1 PG5 1-METHOXY-2-[2-(2-METHOXY-ETHOXY]-ETHANE × 1 VLF 4-methyl-~{N}-[(2~{S})-4-oxidanyl-3-oxidanylidene-1-phenyl-butan-2-yl]benzenesulfonamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.90 Å R-free 0.217
8OFA Crystal structure of human cathepsin L interacting with tosyl phenylalanyl chloromethyl ketone (TPCK) Deposited 2023-03-14 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 114–333（220 aa）
Mutation：T110A TQ8 N-[(2S)-4-chloro-3-oxo-1-phenyl-butan-2-yl]-4-methyl-benzenesulfonamide × 1 EDO 1,2-ETHANEDIOL × 1 PEG DI(HYDROXYETHYL)ETHER × 1 DMS DIMETHYL SULFOXIDE × 2 ACT ACETATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.90 Å R-free 0.217
8OFA Crystal structure of human cathepsin L interacting with tosyl phenylalanyl chloromethyl ketone (TPCK) Deposited 2023-03-14 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 114–333（220 aa）
Mutation：T110A TQ8 N-[(2S)-4-chloro-3-oxo-1-phenyl-butan-2-yl]-4-methyl-benzenesulfonamide × 1 EDO 1,2-ETHANEDIOL × 1 PEG DI(HYDROXYETHYL)ETHER × 3 DMS DIMETHYL SULFOXIDE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.90 Å R-free 0.217
8OFA Crystal structure of human cathepsin L interacting with tosyl phenylalanyl chloromethyl ketone (TPCK) Deposited 2023-03-14 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 114–333（220 aa）
Mutation：T110A TQ8 N-[(2S)-4-chloro-3-oxo-1-phenyl-butan-2-yl]-4-methyl-benzenesulfonamide × 1 EDO 1,2-ETHANEDIOL × 4 PEG DI(HYDROXYETHYL)ETHER × 1 DMS DIMETHYL SULFOXIDE × 2 PGE TRIETHYLENE GLYCOL × 2 VLF 4-methyl-~{N}-[(2~{S})-4-oxidanyl-3-oxidanylidene-1-phenyl-butan-2-yl]benzenesulfonamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.90 Å R-free 0.217
8OZA Human cathepsin L in complex with covalently bound CA-074 methyl ester Deposited 2023-05-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 114–333（220 aa）
Mutation：T110A WRH methyl (2S)-1-[(2S,3S)-3-methyl-2-[[(3S)-3-oxidanyl-4-oxidanylidene-4-(propylamino)butanoyl]amino]pentanoyl]pyrrolidine-2-carboxylate × 1 PEG DI(HYDROXYETHYL)ETHER × 1 EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.80 Å R-free 0.198
8OZA Human cathepsin L in complex with covalently bound CA-074 methyl ester Deposited 2023-05-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 114–333（220 aa）
Mutation：T110A WRH methyl (2S)-1-[(2S,3S)-3-methyl-2-[[(3S)-3-oxidanyl-4-oxidanylidene-4-(propylamino)butanoyl]amino]pentanoyl]pyrrolidine-2-carboxylate × 1 PEG DI(HYDROXYETHYL)ETHER × 1 EDO 1,2-ETHANEDIOL × 2 ACT ACETATE ION × 1 DMS DIMETHYL SULFOXIDE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.80 Å R-free 0.198
8OZA Human cathepsin L in complex with covalently bound CA-074 methyl ester Deposited 2023-05-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 114–333（220 aa）
Mutation：T110A WRH methyl (2S)-1-[(2S,3S)-3-methyl-2-[[(3S)-3-oxidanyl-4-oxidanylidene-4-(propylamino)butanoyl]amino]pentanoyl]pyrrolidine-2-carboxylate × 1 PEG DI(HYDROXYETHYL)ETHER × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.80 Å R-free 0.198
8OZA Human cathepsin L in complex with covalently bound CA-074 methyl ester Deposited 2023-05-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 114–333（220 aa）
Mutation：T110A WRH methyl (2S)-1-[(2S,3S)-3-methyl-2-[[(3S)-3-oxidanyl-4-oxidanylidene-4-(propylamino)butanoyl]amino]pentanoyl]pyrrolidine-2-carboxylate × 1 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.80 Å R-free 0.198
8PRX Crystal structure of human cathepsin L after reaction with the bound ketoamide inhibitor 13b Deposited 2023-07-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 114–333（220 aa）
Chain B 114–333（220 aa）
Chain C 114–333（220 aa）
Chain D 114–333（220 aa）
Mutation：T110A Mutation：T110A Mutation：T110A Mutation：T110A KH0 ~{tert}-butyl ~{N}-[1-[(2~{S})-3-cyclopropyl-1-oxidanylidene-1-[[(2~{S},3~{S})-3-oxidanyl-4-oxidanylidene-1-[(3~{S})-2-oxidanylidenepyrrolidin-3-yl]-4-[(phenylmethyl)amino]butan-2-yl]amino]propan-2-yl]-2-oxidanylidene-pyridin-3-yl]carbamate × 4 DMS DIMETHYL SULFOXIDE × 11 PEG DI(HYDROXYETHYL)ETHER × 8 PG4 TETRAETHYLENE GLYCOL × 1 EDO 1,2-ETHANEDIOL × 10 PGE TRIETHYLENE GLYCOL × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.80 Å R-free 0.203
8QKB Crystal structure of human cathepsin L in complex with the vinyl sulfone inhibitor K777 Deposited 2023-09-14 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 114–333（220 aa）
Chain B 114–333（220 aa）
Chain C 114–333（220 aa）
Chain D 114–333（220 aa）
Mutation：T110A Mutation：T110A Mutation：T110A Mutation：T110A D1R NALPHA-[(4-METHYLPIPERAZIN-1-YL)CARBONYL]-N-{(1S)-3-PHENYL-1-[2-(PHENYLSULFONYL)ETHYL]PROPYL}-L-PHENYLALANINAMIDE × 4 PG4 TETRAETHYLENE GLYCOL × 1 EDO 1,2-ETHANEDIOL × 12 PEG DI(HYDROXYETHYL)ETHER × 5 DMS DIMETHYL SULFOXIDE × 6 PGE TRIETHYLENE GLYCOL × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；293 K；Mature cathepsin L at a concentration of 7 mg/ml was equilibrated against 27% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0. Crystals, which grew at 293 K to final size after approximately 3 days, were transferred to a compound soaking solution containing 22% w/v PEG 8000, 1 mM TCEP and 0.1 M sodium acetate at pH 4.0 as well as 5% v/v DMSO and 10% v/v PEG 400.
Resolution 1.60 Å R-free 0.187
8UAC CATHEPSIN L IN COMPLEX WITH AC1115 Deposited 2023-09-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 114–333（220 aa）
Chain B 114–333（220 aa）
Not recorded W28 N-[(2S)-1-({(2S)-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}amino)-4-methyl-1-oxopentan-2-yl]-1H-indole-2-carboxamide × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；291 K；0.1 M NaAc, pH 5.5, 25% PEG 3350
Resolution 1.40 Å R-free 0.239

63 other PDB entries and 156 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CATL_HUMAN
Isoform —
PDB entities 2
Chains and sequence ranges Author chain B； PDBConstruct 1–221； UniProt 113–333

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 2nqd

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2nqd
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2nqd
Deposition date deposition_date2006-10-31
Structure title titleCrystal structure of cysteine protease inhibitor, chagasin, in complex with human cathepsin L
Keywords keywordschagasin-cathepsin L complex, three prong inhibition mode, HYDROLASE INHIBITOR-HYDROLASE COMPLEX; HYDROLASE INHIBITOR/HYDROLASE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier22.40 Å
Radius of gyration Rg (electron density) rg_electron21.85 Å
Forward intensity I(0) i024511900.00
Molecular weight molecular_weight36628.0 kDa
Excluded volume excluded_volume45230 ų
Envelope volume envelope_volume52963 ų
Hydration-shell volume shell_volume21117 ų
Envelope diameter envelope_diameter84.0 Å
Shell Rg shell_rg27.72 Å
Envelope Rg envelope_rg22.34 Å
Shape Rg shape_rg21.81 Å
Total Rg total_rg22.72 Å
Total atoms total_atoms2578
Residues n_residues329
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax79.1 Å
Rg (real space) rg_real22.48 Å
Rg uncertainty (real space) rg_real_error0.77 Å
I(0) (real space) i0_real2.4510e+07
I(0) uncertainty (real space) i0_real_error3.4850e+05
Rg (reciprocal space) rg_reciprocal22.46 Å
I(0) (reciprocal space) i0_reciprocal24510000.0000
Solution quality estimate total_estimate0.7730
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary24.0 Å
Skewness Skewness skewness0.493
Kurtosis Kurtosis kurtosis-0.127
Angular range angular_range— – 0.3550 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7665000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.709; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.920; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (6)

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2nqda_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.26 — ICP-like
Family Family familyb.1.26.1 — ICP-like
Domain ID domain_idd2nqdb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.3 — Cysteine proteinases
Superfamily Superfamily superfamilyd.3.1 — Cysteine proteinases
Family Family familyd.3.1.0 — automated matches

CATH v4.4 (2 domains)

Domain ID domain_id2nqdA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily2020 —
Domain ID domain_id2nqdB00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology70 — Cathepsin B; Chain A
Homologous superfamily homologous superfamily10 — Cysteine proteinases
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8. Citations (1)

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9. Files and Curves (10)