› 1yny

X-ray diffraction
2.3Å resolution

Molecular Structure of D-Hydantoinase from a Bacillus sp. AR9: Evidence for mercury inhibition

Released:
DOI: 10.2210/pdb1yny/pdb
PDB entry 1yny coloured by chain, front view.
PDB entry 1yny coloured by chain, side view.
PDB entry 1yny coloured by chain, top view.
Source organism: Bacillus sp. AR9
Primary publication:
Molecular structure of D-hydantoinase from Bacillus sp. AR9: evidence for mercury inhibition.
Radha Kishan KV, Vohra RM, Ganesan K, Agrawal V, Sharma VM, Sharma R
J Mol Biol 347 95-105 (2005)
PMID: 15733920

Function and Biology Details

Reaction catalysed: 
5,6-dihydrouracil + H(2)O = 3-ureidopropanoate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176974 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Amidohydrolase-related domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 461 amino acids
Theoretical weight: 50.47 KDa
Source organism: Bacillus sp. AR9
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5DLU2 (Residues: 1-461; Coverage: 100%)
Sequence domains: Amidohydrolase family
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand MN 4 x MN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P64
Unit cell:
a: 129.54Å b: 129.54Å c: 102.85Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.199 0.199 0.243
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Beyond gene expression: the impact of protein post-translational modifications in bacteria.
Cain et al. (2014)
9 other articles

1 mention without citation

Crystallization and preliminary crystallographic studies of the recombinant dihydropyrimidinase from Sinorhizobium meliloti CECT4114.
Martínez-Rodríguez et al. (2006)