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5wot

NMR solution structure of a-lytic protease using two 4D-spectra

Method: SOLUTION NMR Dmax: 47.9 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Alpha-lytic protease

OrganismNot specified

UniProt P00778

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 200–397 Fragment：residues 200-397 No other associated polymer SOLUTION NMR NMR measurement conditions：pH 4；298 K；Ionic strength (raw mmCIF value) 50；Pressure 1 NMR sample composition：2.0 mM [U-13C; U-15N] alpha-lytic protease protein, 92% H2O/8% D2O | 92% H2O/8% D2O Resolution not provided

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 5WOT Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1BOQ PRO REGION C-TERMINUS: PROTEASE ACTIVE SITE INTERACTIONS ARE CRITICAL IN CATALYZING THE FOLDING OF ALPHA-LYTIC PROTEASE Deposited 1998-08-05 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 200–397（198 aa）
Mutation：V119I SO4 SULFATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8；pH 8.0
Resolution 2.10 Å R-free 0.236
1GBA ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY ALA Deposited 1995-09-06 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 200–397（198 aa）
Mutation：M190A, G216A SO4 SULFATE ION × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.15 Å
1GBB Alpha-lytic protease with met 190 replaced by ALA AND GLY 216 replaced by ALA complex with METHOXYSUCCINYL-ALA-ALA-PRO-ALANINE BORONIC ACID Deposited 1995-09-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 200–397（198 aa）
Mutation：M190A, G216A SO4 SULFATE ION × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.15 Å
1GBC ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY ALA COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-LEUCINE BORONIC ACID Deposited 1995-09-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 200–397（198 aa）
Mutation：M190A, G216A SO4 SULFATE ION × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.20 Å
1GBD ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY ALA COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-PHENYLALANINE BORONIC ACID Deposited 1995-09-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 200–397（198 aa）
Mutation：M190A, G216A SO4 SULFATE ION × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.20 Å
1GBE ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY LEU Deposited 1995-09-06 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 200–397（198 aa）
Mutation：M190A, G216L SO4 SULFATE ION × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.30 Å
1GBF ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY LEU COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-ALANINE BORONIC ACID Deposited 1995-09-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 200–397（198 aa）
Mutation：M190A, G216L SO4 SULFATE ION × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.15 Å
1GBH ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY LEU COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-LEUCINE BORONIC ACID Deposited 1995-09-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 200–397（198 aa）
Mutation：M190A, G216L SO4 SULFATE ION × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.20 Å
1GBI ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY LEU COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-PHENYLALANINE BORONIC ACID Deposited 1995-09-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 200–397（198 aa）
Mutation：M190A, G216L SO4 SULFATE ION × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.30 Å
1GBJ ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA Deposited 1995-09-06 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 200–397（198 aa）
Mutation：M190A SO4 SULFATE ION × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.00 Å
1GBK ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-ALANINE BORONIC ACID Deposited 1995-09-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 200–397（198 aa）
Mutation：M190A SO4 SULFATE ION × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.13 Å
1GBL ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-LEUCINE BORONIC ACID Deposited 1995-09-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 200–397（198 aa）
Mutation：M190A SO4 SULFATE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.15 Å
1GBM ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-PHENYLALANINE BORONIC ACID Deposited 1995-09-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 200–397（198 aa）
Mutation：M190A SO4 SULFATE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.28 Å
1P01 Serine protease mechanism. structure of an inhibitory complex oF ALPHA-LYTIC Protease and a tightly bound peptide boronic acid Deposited 1989-04-24 Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 200–397（198 aa）
Not recorded 0EG N-(tert-butoxycarbonyl)-L-alanyl-N-[(1R)-1-(dihydroxyboranyl)-2-methylpropyl]-L-prolinamide × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.00 Å
1P02 STRUCTURE ANALYSIS OF SPECIFICITY. ALPHA-LYTIC PROTEASE COMPLEXES WITH ANALOGUES OF REACTION INTERMEDIATES Deposited 1989-04-24 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 200–397（198 aa）
Not recorded SO4 SULFATE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.00 Å
1P03 STRUCTURE ANALYSIS OF SPECIFICITY. ALPHA-LYTIC PROTEASE COMPLEXES WITH ANALOGUES OF REACTION INTERMEDIATES Deposited 1989-04-24 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 200–397（198 aa）
Not recorded SO4 SULFATE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.15 Å
1P04 STRUCTURE ANALYSIS OF SPECIFICITY. ALPHA-LYTIC PROTEASE COMPLEXES WITH ANALOGUES OF REACTION INTERMEDIATES Deposited 1989-04-24 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 200–397（198 aa）
Not recorded SO4 SULFATE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.55 Å
1P05 STRUCTURE ANALYSIS OF SPECIFICITY. ALPHA-LYTIC PROTEASE COMPLEXES WITH ANALOGUES OF REACTION INTERMEDIATES Deposited 1989-04-24 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 200–397（198 aa）
Not recorded SO4 SULFATE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.10 Å
1P06 STRUCTURE ANALYSIS OF SPECIFICITY. ALPHA-LYTIC PROTEASE COMPLEXES WITH ANALOGUES OF REACTION INTERMEDIATES Deposited 1989-04-24 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 200–397（198 aa）
Not recorded SO4 SULFATE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.34 Å
1P09 STRUCTURAL PLASTICITY AS A DETERMINANT OF ENZYME SPECIFICITY. CREATING BROADLY SPECIFIC PROTEASES Deposited 1989-04-24 Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 200–397（198 aa）
Not recorded SO4 SULFATE ION × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.20 Å
1P10 STRUCTURAL PLASTICITY AS A DETERMINANT OF ENZYME SPECIFICITY. CREATING BROADLY SPECIFIC PROTEASES Deposited 1989-04-24 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 200–397（198 aa）
Not recorded SO4 SULFATE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.25 Å
1P11 CRYSTAL STRUCTURES OF ALPHA-LYTIC PROTEASE COMPLEXES WITH IRREVERSIBLY BOUND PHOSPHONATE ESTERS Deposited 1990-10-26 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain E 200–397（198 aa）
Not recorded SO4 SULFATE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.93 Å
1P12 CRYSTAL STRUCTURES OF ALPHA-LYTIC PROTEASE COMPLEXES WITH IRREVERSIBLY BOUND PHOSPHONATE ESTERS Deposited 1990-10-26 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain E 200–397（198 aa）
Not recorded SO4 SULFATE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.90 Å
1QQ4 CRYSTAL STRUCTURE OF AN ALPHA-LYTIC PROTEASE MUTANT WITH ACCELERATED FOLDING KINETICS, R102H/G134S Deposited 1999-06-10 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 200–397（198 aa） Fragment：RESIDUES 1-198
Mutation：R102H,G134S SO4 SULFATE ION × 5 GOL GLYCEROL × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.14；298 K；lithium sulfate, tris-sulfate, pH 5.14, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.20 Å R-free 0.174
1QRW CRYSTAL STRUCTURE OF AN ALPHA-LYTIC PROTEASE MUTANT WITH ACCELERATED FOLDING KINETICS, R102H/G134S, PH 8 Deposited 1999-06-16 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 200–397（198 aa） Fragment：MATURE PROTEASE DOMAIN, RESIDUES 1-198
Mutation：R102H,G134S SO4 SULFATE ION × 4 GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；LITHIUM SULFATE, TRIS-SULFATE, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.20 Å R-free 0.181
1QRX CRYSTAL STRUCTURE OF WILD-TYPE ALPHA-LYTIC PROTEASE AT 1.6 A, PH 5.14 Deposited 1999-06-16 Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 200–397（198 aa） Fragment：MATURE PROTEASE DOMAIN, RESIDUES 1-198
Not recorded SO4 SULFATE ION × 3 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.14；298 K；LITHIUM SULFATE, TRIS-SULFATE, pH 5.14, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.60 Å R-free 0.169
1SSX 0.83A resolution crystal structure of alpha-lytic protease at pH 8 Deposited 2004-03-24 Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 200–397（198 aa） Fragment：Mature protease domain (residues 200-397)
Not recorded SO4 SULFATE ION × 4 GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；1.3M lithium sulfate, 0.02M Tris, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 0.83 Å R-free 0.099
1TAL ALPHA-LYTIC PROTEASE AT 120 K (SINGLE STRUCTURE MODEL) Deposited 1996-10-30 Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 200–397（198 aa）
Not recorded SO4 SULFATE ION × 3 TAM TRIS(HYDROXYETHYL)AMINOMETHANE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8；pH 8.0
Resolution 1.50 Å R-free 0.192
2ALP REFINED STRUCTURE OF ALPHA-LYTIC PROTEASE AT 1.7 ANGSTROMS RESOLUTION. ANALYSIS OF HYDROGEN BONDING AND SOLVENT STRUCTURE Deposited 1985-03-07 Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 200–397（198 aa）
Not recorded SO4 SULFATE ION × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.70 Å
2H5C 0.82A resolution crystal structure of alpha-lytic protease at pH 5 Deposited 2006-05-25 Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 200–397（198 aa） Fragment：MATURE PROTEASE DOMAIN (RESIDUES 200-397)
Not recorded SO4 SULFATE ION × 11 GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 4.25；298 K；1.3M LITHIUM SULFATE, 0.02M TRIS, PH 4.25, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
Resolution 0.82 Å R-free 0.093
2H5D 0.9A resolution crystal structure of alpha-lytic protease complexed with a transition state analogue, MeOSuc-Ala-Ala-Pro-Val boronic acid Deposited 2006-05-25 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 200–397（198 aa） Fragment：MATURE PROTEASE DOMAIN (RESIDUES 200-397)
Not recorded SO4 SULFATE ION × 8 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8；298 K；1.3M LITHIUM SULFATE, 0.02M TRIS, PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K, pH 8.00
Resolution 0.90 Å R-free 0.091
2LPR STRUCTURAL BASIS FOR BROAD SPECIFICITY IN ALPHA-LYTIC PROTEASE MUTANTS Deposited 1991-08-05 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 200–397（198 aa）
Not recorded SO4 SULFATE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.25 Å
2PRO PRO REGION OF ALPHA-LYTIC PROTEASE Deposited 1998-08-20 Different construct Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 34–199（166 aa） Fragment：PRO REGION
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 8；pH 8.0
Resolution 3.00 Å R-free 0.342
2PRO PRO REGION OF ALPHA-LYTIC PROTEASE Deposited 1998-08-20 Different construct Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 34–199（166 aa） Fragment：PRO REGION
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 8；pH 8.0
Resolution 3.00 Å R-free 0.342
2PRO PRO REGION OF ALPHA-LYTIC PROTEASE Deposited 1998-08-20 Different construct Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 34–199（166 aa） Fragment：PRO REGION
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 8；pH 8.0
Resolution 3.00 Å R-free 0.342
2PRO PRO REGION OF ALPHA-LYTIC PROTEASE Deposited 1998-08-20 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric
Chain A 34–199（166 aa） Fragment：PRO REGION
Chain B 34–199（166 aa） Fragment：PRO REGION
Chain C 34–199（166 aa） Fragment：PRO REGION
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 8；pH 8.0
Resolution 3.00 Å R-free 0.342
2ULL MULTIPLE CONFORMATION STRUCTURE OF ALPHA-LYTIC PROTEASE AT 120 K Deposited 1996-11-26 Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 200–397（198 aa）
Not recorded SO4 SULFATE ION × 3 TAM TRIS(HYDROXYETHYL)AMINOMETHANE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8；pH 8.0
Resolution 1.50 Å R-free 0.192
3LPR STRUCTURAL BASIS FOR BROAD SPECIFICITY IN ALPHA-LYTIC PROTEASE MUTANTS Deposited 1991-08-05 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 200–397（198 aa）
Not recorded SO4 SULFATE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.15 Å
3M7T Crystal Structure of Alpha-Lytic Protease SB2+3 E8A/R105S Mutant Deposited 2010-03-17 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 200–397（198 aa） Fragment：MATURE PROTEASE DOMAIN (RESIDUES 1-198)
Mutation：E8A, R105S GOL GLYCEROL × 1 SO4 SULFATE ION × 5 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；277 K；1.3 M lithium sulfate, 20 mM Tris sulfate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 1.55 Å R-free 0.202
3M7U Crystal Structure of Alpha-Lytic Protease SB1+2 R64A/E182Q Mutant Deposited 2010-03-17 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 200–397（198 aa） Fragment：MATURE PROTEASE DOMAIN (RESIDUES 1-198)
Mutation：R64A, E182Q SO4 SULFATE ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；277 K；1.3 M lithium sulfate, 20 mM Tris sulfate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 1.05 Å R-free 0.164
3PRO ALPHA-LYTIC PROTEASE COMPLEXED WITH C-TERMINAL TRUNCATED PRO REGION Deposited 1998-08-26 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 200–397（198 aa） Fragment：MATURE PROTEASE
Chain C 34–199（166 aa） Fragment：PRO REGION
Mutation：M158A AES 4-(2-AMINOETHYL)BENZENESULFONYL FLUORIDE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.25；pH 6.25
Resolution 1.80 Å R-free 0.230
3PRO ALPHA-LYTIC PROTEASE COMPLEXED WITH C-TERMINAL TRUNCATED PRO REGION Deposited 1998-08-26 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain B 200–397（198 aa） Fragment：MATURE PROTEASE
Chain D 34–199（166 aa） Fragment：PRO REGION
Mutation：M158A AES 4-(2-AMINOETHYL)BENZENESULFONYL FLUORIDE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.25；pH 6.25
Resolution 1.80 Å R-free 0.230
3QGJ 1.3A Structure of alpha-Lytic Protease Bound to Ac-AlaAlaPro-Alanal Deposited 2011-01-24 Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 200–397（198 aa） Fragment：residues 200-397
Not recorded EDO 1,2-ETHANEDIOL × 3 SO4 SULFATE ION × 4 TFA trifluoroacetic acid × 3 X-RAY DIFFRACTION
X-ray crystallization conditions pH 4.8；277 K；1.2M Li2SO4, 20mM Tris-SO4, pH 4.8, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 1.30 Å R-free 0.192
3QGJ 1.3A Structure of alpha-Lytic Protease Bound to Ac-AlaAlaPro-Alanal Deposited 2011-01-24 Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 200–397（198 aa） Fragment：residues 200-397
Not recorded EDO 1,2-ETHANEDIOL × 2 SO4 SULFATE ION × 3 TFA trifluoroacetic acid × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 4.8；277 K；1.2M Li2SO4, 20mM Tris-SO4, pH 4.8, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 1.30 Å R-free 0.192
3QGJ 1.3A Structure of alpha-Lytic Protease Bound to Ac-AlaAlaPro-Alanal Deposited 2011-01-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain A 200–397（198 aa） Fragment：residues 200-397
Chain C 200–397（198 aa） Fragment：residues 200-397
Not recorded EDO 1,2-ETHANEDIOL × 10 SO4 SULFATE ION × 14 TFA trifluoroacetic acid × 8 X-RAY DIFFRACTION
X-ray crystallization conditions pH 4.8；277 K；1.2M Li2SO4, 20mM Tris-SO4, pH 4.8, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 1.30 Å R-free 0.192
3URC T181G mutant of alpha-Lytic Protease Deposited 2011-11-22 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 200–397（198 aa）
Mutation：T181G SO4 SULFATE ION × 2 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；1.3 M lithium sulfate and 20 mM Tris sulfate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.10 Å R-free 0.136
3URD T181A mutant of alpha-Lytic Protease Deposited 2011-11-22 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 200–397（198 aa） Fragment：UNP residues 200-397
Mutation：T132A SO4 SULFATE ION × 5 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；1.3 M lithium sulfate and 20 mM Tris sulfate, pH 8.0 , VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.08 Å R-free 0.142
3URE Repack mutant (T181I, W199L, Q210I) of alpha-Lytic Protease Deposited 2011-11-22 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 200–397（198 aa）
Mutation：T181I, W199L, Q210I SO4 SULFATE ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；1.3 M lithium sulfate, 10 mM CuCl2, and 20 mM Tris sulfate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.49 Å R-free 0.170
3URE Repack mutant (T181I, W199L, Q210I) of alpha-Lytic Protease Deposited 2011-11-22 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 200–397（198 aa）
Mutation：T181I, W199L, Q210I SO4 SULFATE ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；1.3 M lithium sulfate, 10 mM CuCl2, and 20 mM Tris sulfate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.49 Å R-free 0.170
4PRO ALPHA-LYTIC PROTEASE COMPLEXED WITH PRO REGION Deposited 1998-10-01 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 200–397（198 aa） Fragment：CHAIN A, B, MATURE PROTEASE. CHAIN C, D, PRO REGION
Chain C 34–199（166 aa） Fragment：CHAIN A, B, MATURE PROTEASE. CHAIN C, D, PRO REGION
Mutation：CHAIN A, B, M158A Mutation：CHAIN A, B, M158A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；pH 6.5
Resolution 2.40 Å R-free 0.238
4PRO ALPHA-LYTIC PROTEASE COMPLEXED WITH PRO REGION Deposited 1998-10-01 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain B 200–397（198 aa） Fragment：CHAIN A, B, MATURE PROTEASE. CHAIN C, D, PRO REGION
Chain D 34–199（166 aa） Fragment：CHAIN A, B, MATURE PROTEASE. CHAIN C, D, PRO REGION
Mutation：CHAIN A, B, M158A Mutation：CHAIN A, B, M158A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；pH 6.5
Resolution 2.40 Å R-free 0.238
5LPR STRUCTURAL BASIS FOR BROAD SPECIFICITY IN ALPHA-LYTIC PROTEASE MUTANTS Deposited 1991-08-05 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 200–397（198 aa）
Not recorded SO4 SULFATE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.13 Å
6LPR STRUCTURAL BASIS FOR BROAD SPECIFICITY IN ALPHA-LYTIC PROTEASE MUTANTS Deposited 1991-08-05 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 200–397（198 aa）
Not recorded SO4 SULFATE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.10 Å
7LPR STRUCTURAL BASIS FOR BROAD SPECIFICITY IN ALPHA-LYTIC PROTEASE MUTANTS Deposited 1991-08-05 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 200–397（198 aa）
Not recorded SO4 SULFATE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.05 Å
8LPR STRUCTURAL BASIS FOR BROAD SPECIFICITY IN ALPHA-LYTIC PROTEASE MUTANTS Deposited 1991-08-05 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 200–397（198 aa）
Not recorded SO4 SULFATE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.25 Å
9LPR STRUCTURAL BASIS FOR BROAD SPECIFICITY IN ALPHA-LYTIC PROTEASE MUTANTS Deposited 1991-08-05 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 200–397（198 aa）
Not recorded SO4 SULFATE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.20 Å

48 other PDB entries and 56 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PRLA_LYSEN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–198； UniProt 200–397

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

SAXS scattering curve SAXS Profile

SAXS profile for 5wot

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5wot
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5wot
Deposition date deposition_date2017-08-03
Structure title titleNMR solution structure of a-lytic protease using two 4D-spectra
Keywords keywordsprotease, HYDROLASE; HYDROLASE
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier15.44 Å
Radius of gyration Rg (electron density) rg_electron15.13 Å
Forward intensity I(0) i0640229000.00
Molecular weight molecular_weight198680.0 kDa
Excluded volume excluded_volume243100 ų
Envelope volume envelope_volume35175 ų
Hydration-shell volume shell_volume17627 ų
Envelope diameter envelope_diameter52.9 Å
Shell Rg shell_rg22.93 Å
Envelope Rg envelope_rg16.53 Å
Shape Rg shape_rg15.10 Å
Total Rg total_rg15.38 Å
Total atoms total_atoms27550
Residues n_residues1980
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax47.9 Å
Rg (real space) rg_real15.32 Å
Rg uncertainty (real space) rg_real_error0.27 Å
I(0) (real space) i0_real6.4020e+08
I(0) uncertainty (real space) i0_real_error7.8160e+06
Rg (reciprocal space) rg_reciprocal15.33 Å
I(0) (reciprocal space) i0_reciprocal640200000.0000
Solution quality estimate total_estimate0.8922
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.2 Å
Skewness Skewness skewness0.089
Kurtosis Kurtosis kurtosis-0.423
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1598000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.878; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.978
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd5wota_
Class classb — All beta proteins
Fold Fold foldb.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamilyb.47.1 — Trypsin-like serine proteases
Family Family familyb.47.1.1 — Prokaryotic proteases

CATH v4.4 (2 domains)

Domain ID domain_id5wotA01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id5wotA02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
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8. Citations (1)

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9. Files and Curves (10)