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2pro

PRO REGION OF ALPHA-LYTIC PROTEASE

Method: X-RAY DIFFRACTION Dmax: 97.1 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

ALPHA-LYTIC PROTEASE

Lysobacter enzymogenes

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 34–199 Fragment：PRO REGION No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：pH 8；pH 8.0 Resolution 3.00 Å R-free 0.342
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain B； UniProt 34–199 Fragment：PRO REGION No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：pH 8；pH 8.0 Resolution 3.00 Å R-free 0.342
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain C； UniProt 34–199 Fragment：PRO REGION No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：pH 8；pH 8.0 Resolution 3.00 Å R-free 0.342
4 Protein homooligomer Homooligomer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count Chain A； UniProt 34–199 Chain B； UniProt 34–199 Chain C； UniProt 34–199 Fragment：PRO REGION No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：pH 8；pH 8.0 Resolution 3.00 Å R-free 0.342

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 2PRO 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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
2ULL MULTIPLE CONFORMATION STRUCTURE OF ALPHA-LYTIC PROTEASE AT 120 K Deposited 1996-11-26 Different construct Different ligand/ion 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 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 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 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 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 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 construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 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 construct Different oligomeric state Different ligand/ion 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 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 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 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 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 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 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 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 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
5WOT NMR solution structure of a-lytic protease using two 4D-spectra Deposited 2017-08-03 Different construct 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 200-397
Not recorded No recorded non-water small molecule 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
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 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 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 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 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 53 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 1–166； UniProt 34–199 Author chain B； PDBConstruct 1–166； UniProt 34–199 Author chain C； PDBConstruct 1–166； UniProt 34–199

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 2pro

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2pro
Deposition date deposition_date1998-08-20
Structure title titlePRO REGION OF ALPHA-LYTIC PROTEASE
Keywords keywordsPRO REGION, FOLDASE, PROTEIN FOLDING, SERINE PROTEASE; PRO REGION
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier29.22 Å
Radius of gyration Rg (electron density) rg_electron28.94 Å
Forward intensity I(0) i034998400.00
Molecular weight molecular_weight44514.0 kDa
Excluded volume excluded_volume55209 ų
Envelope volume envelope_volume75371 ų
Hydration-shell volume shell_volume23367 ų
Envelope diameter envelope_diameter96.5 Å
Shell Rg shell_rg33.69 Å
Envelope Rg envelope_rg28.39 Å
Shape Rg shape_rg28.94 Å
Total Rg total_rg29.46 Å
Total atoms total_atoms3139
Residues n_residues414
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 dmax97.1 Å
Rg (real space) rg_real29.27 Å
Rg uncertainty (real space) rg_real_error0.87 Å
I(0) (real space) i0_real3.5000e+07
I(0) uncertainty (real space) i0_real_error5.3850e+05
Rg (reciprocal space) rg_reciprocal29.26 Å
I(0) (reciprocal space) i0_reciprocal35000000.0000
Solution quality estimate total_estimate0.8971
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.1 Å
Skewness Skewness skewness0.284
Kurtosis Kurtosis kurtosis-0.544
Angular range angular_range— – 0.2700 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1802000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.929; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.942; Smooth: 0.929
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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) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd2proa1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.52 — Alpha-lytic protease prodomain-like
Superfamily Superfamily superfamilyd.52.1 — Alpha-lytic protease prodomain
Family Family familyd.52.1.1 — Alpha-lytic protease prodomain
Domain ID domain_idd2proa2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.52 — Alpha-lytic protease prodomain-like
Superfamily Superfamily superfamilyd.52.1 — Alpha-lytic protease prodomain
Family Family familyd.52.1.1 — Alpha-lytic protease prodomain
Domain ID domain_idd2prob1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.52 — Alpha-lytic protease prodomain-like
Superfamily Superfamily superfamilyd.52.1 — Alpha-lytic protease prodomain
Family Family familyd.52.1.1 — Alpha-lytic protease prodomain
Domain ID domain_idd2prob2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.52 — Alpha-lytic protease prodomain-like
Superfamily Superfamily superfamilyd.52.1 — Alpha-lytic protease prodomain
Family Family familyd.52.1.1 — Alpha-lytic protease prodomain
Domain ID domain_idd2proc1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.52 — Alpha-lytic protease prodomain-like
Superfamily Superfamily superfamilyd.52.1 — Alpha-lytic protease prodomain
Family Family familyd.52.1.1 — Alpha-lytic protease prodomain
Domain ID domain_idd2proc2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.52 — Alpha-lytic protease prodomain-like
Superfamily Superfamily superfamilyd.52.1 — Alpha-lytic protease prodomain
Family Family familyd.52.1.1 — Alpha-lytic protease prodomain

CATH v4.4 (6 domains)

Domain ID domain_id2proA01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology300 — GMP Synthetase; Chain A, domain 3
Homologous superfamily homologous superfamily50 —
Domain ID domain_id2proA02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology300 — GMP Synthetase; Chain A, domain 3
Homologous superfamily homologous superfamily50 —
Domain ID domain_id2proB01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology300 — GMP Synthetase; Chain A, domain 3
Homologous superfamily homologous superfamily50 —
Domain ID domain_id2proB02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology300 — GMP Synthetase; Chain A, domain 3
Homologous superfamily homologous superfamily50 —
Domain ID domain_id2proC01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology300 — GMP Synthetase; Chain A, domain 3
Homologous superfamily homologous superfamily50 —
Domain ID domain_id2proC02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology300 — GMP Synthetase; Chain A, domain 3
Homologous superfamily homologous superfamily50 —
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8. Citations (1)

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9. Files and Curves (10)