› 1q5p

X-ray diffraction
1.6Å resolution

S156E/S166D variant of Bacillus lentus subtilisin

Released:
DOI: 10.2210/pdb1q5p/pdb
PDB entry 1q5p coloured by chain, front view.
PDB entry 1q5p coloured by chain, side view.
PDB entry 1q5p coloured by chain, top view.
Source organism: Lederbergia lenta
Primary publication:
Do enzymes change the nature of transition states? Mapping the transition state for general acid-base catalysis of a serine protease.
Bott RR, Chan G, Domingo B, Ganshaw G, Hsia CY, Knapp M, Murray CJ
Biochemistry 42 10545-53 (2003)
PMID: 12962477

Function and Biology Details

Reaction catalysed: 
Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151551 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Subtilisin Savinase Chain: A
Molecule details ›
Chain: A
Length: 269 amino acids
Theoretical weight: 26.94 KDa
Source organism: Lederbergia lenta
Expression system: Bacillus subtilis
UniProt:
  • Canonical: P29600 (Residues: 1-269; Coverage: 100%)
Sequence domains: Subtilase family
Structure domains: Peptidase S8/S53 domain

Ligands and Environments

2 bound ligands:
Ligand SO4 1 x SO4
Ligand CA 2 x CA
1 modified residue:
Ligand SEB 1 x SEB

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 53.45Å b: 61.5Å c: 75.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 0.168 not available
Expression system: Bacillus subtilis

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Citations

9 citation in other articles

Dissection of the stepwise mechanism to beta-lactam formation and elucidation of a rate-determining conformational change in beta-lactam synthetase.
Raber et al. (2009)
8 more