HUMAN PROCATHEPSIN L
Homo sapiens
State in the Current Structure
| Assembly | Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Associated Components | Method and Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|
| 1 | Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count | Chain A； UniProt 18–333 | Mutation：T110A Non-standard monomer：Yes (specific site not provided by mmCIF) | No other associated polymer | 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 |
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 1CS8 | 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 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 |
| 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 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 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 |
| 2NQD Crystal structure of cysteine protease inhibitor, chagasin, in complex with human cathepsin L Deposited 2006-10-31 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric |
Chain B
113–333（221 aa）
Fragment：residues 1-220
|
Mutation：C25A | 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 |
| 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 oligomeric state 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 mutation/modification 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 mutation/modification 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–316； UniProt 18–333 |
