› 1och

X-ray diffraction
1.8Å resolution

Crystal structure of the S155C mutant of malonamidase E2 from Bradyrhizobium japonicum

Released:
DOI: 10.2210/pdb1och/pdb
PDB entry 1och coloured by chain, front view.
PDB entry 1och coloured by chain, side view.
PDB entry 1och coloured by chain, top view.
Source organism: Bradyrhizobium japonicum
Primary publication:
Characterization of a novel Ser-cisSer-Lys catalytic triad in comparison with the classical Ser-His-Asp triad.
Shin S, Yun YS, Koo HM, Kim YS, Choi KY, Oh BH
J Biol Chem 278 24937-43 (2003)
PMID: 12711609

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195661 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Amidase domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 414 amino acids
Theoretical weight: 43.78 KDa
Source organism: Bradyrhizobium japonicum
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9ZIV5 (Residues: 1-414; Coverage: 100%)
Sequence domains: Amidase
Structure domains: Amidase signature (AS) domain

Ligands and Environments

No bound ligands
1 modified residue:
Ligand CSD 2 x CSD

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P21212
Unit cell:
a: 103.606Å b: 94.985Å c: 74.921Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.194 0.237
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Structure and function of fatty acid amide hydrolase.
McKinney et al. (2005)
4 more