› 3wwx

X-ray diffraction
1.49Å resolution

Crystal structure of D-stereospecific amidohydrolase from Streptomyces sp. 82F2

Released:
DOI: 10.2210/pdb3wwx/pdb
PDB entry 3wwx coloured by chain, front view.
PDB entry 3wwx coloured by chain, side view.
PDB entry 3wwx coloured by chain, top view.
Source organism: Streptomyces sp. 82F2
Primary publication:
Crystal structure of D-stereospecific amidohydrolase from Streptomyces sp. 82F2 - insight into the structural factors for substrate specificity.
Arima J, Shimone K, Miyatani K, Tsunehara Y, Isoda Y, Hino T, Nagano S
FEBS J 283 337-49 (2016)
PMID: 26513520

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-122865 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase-related domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 349 amino acids
Theoretical weight: 37.44 KDa
Source organism: Streptomyces sp. 82F2
Expression system: Escherichia coli
UniProt:
  • Canonical: E2RVJ1 (Residues: 34-382; Coverage: 99%)
Gene name: s12ap
Sequence domains: Beta-lactamase
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

1 bound ligand:
Ligand DIA 1 x DIA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B1
Spacegroup: P212121
Unit cell:
a: 59.29Å b: 74.681Å c: 76.447Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.149 0.141 0.162
Expression system: Escherichia coli

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Citations

3 citation in other articles

Systematic Structure-Based Search for Ochratoxin-Degrading Enzymes in Proteomes from Filamentous Fungi.
Leitão et al. (2021)
2 more

2 mentions without citation

Crystal structure of D-stereospecific amidohydrolase from Streptomyces sp. 82F2 - insight into the structural factors for substrate specificity.
Arima et al. (2016)
1 more