› 1c4x

X-ray diffraction
2.4Å resolution

2-HYDROXY-6-OXO-6-PHENYLHEXA-2,4-DIENOATE HYDROLASE (BPHD) FROM RHODOCOCCUS SP. STRAIN RHA1

Released:
DOI: 10.2210/pdb1c4x/pdb
PDB entry 1c4x coloured by chain, front view.
PDB entry 1c4x coloured by chain, side view.
PDB entry 1c4x coloured by chain, top view.
Source organism: Rhodococcus jostii RHA1
Primary publication:
Three-Dimensional Structure of Microbial 2-Hydroxyl-6-Oxo-6-Phenylhexa-2,4- Dienoic Acid (Hpda) Hydrolase (Bphd Enzyme) from Rhodococcus Sp. Strain Rha1, in the Pcb Degradation Pathway
Nandhagopal N, Senda T, Hatta T, Yamada A, Masai E, Fukuda M, Mitsui Y
Proc. Jpn. Acad., Ser. B, Phys. Biol. Sci. 73 154- (1997)

Function and Biology Details

Reaction catalysed: 
2,6-dioxo-6-phenylhexa-3-enoate + H(2)O = benzoate + 2-oxopent-4-enoate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181129 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
AB hydrolase-1 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 285 amino acids
Theoretical weight: 31.68 KDa
Source organism: Rhodococcus jostii RHA1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q75WN8 (Residues: 1-285; Coverage: 100%)
Gene names: RHA1_ro10136, bphD, bphD1
Sequence domains: Alpha/beta hydrolase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: I422
Unit cell:
a: 110.8Å b: 110.8Å c: 136.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.178 0.227
Expression system: Escherichia coli

Quick links

Citations

7 mentions without citation

Crystal structures of RsbQ, a stress-response regulator in Bacillus subtilis.
Kaneko et al. (2005)
6 more