› 1gq6

X-ray diffraction
1.75Å resolution

PROCLAVAMINATE AMIDINO HYDROLASE FROM STREPTOMYCES CLAVULIGERUS

Released:
DOI: 10.2210/pdb1gq6/pdb
PDB entry 1gq6 coloured by chain, front view.
PDB entry 1gq6 coloured by chain, side view.
PDB entry 1gq6 coloured by chain, top view.
Source organism: Streptomyces clavuligerus
Primary publication:
Oligomeric structure of proclavaminic acid amidino hydrolase: evolution of a hydrolytic enzyme in clavulanic acid biosynthesis.
Elkins JM, Clifton IJ, Hernández H, Doan LX, Robinson CV, Schofield CJ, Hewitson KS
Biochem J 366 423-34 (2002)
PMID: 12020346

Function and Biology Details

Reaction catalysed: 
Amidinoproclavaminate + H(2)O = proclavaminate + urea
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-143598 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Proclavaminate amidinohydrolase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 313 amino acids
Theoretical weight: 33.44 KDa
Source organism: Streptomyces clavuligerus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0DJQ3 (Residues: 1-313; Coverage: 100%)
Gene name: pah
Sequence domains: Arginase family
Structure domains: Ureohydrolase domain

Ligands and Environments

1 bound ligand:
Ligand MN 6 x MN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: C2
Unit cell:
a: 139.859Å b: 78.931Å c: 93.199Å
α: 90° β: 123.9° γ: 90°
R-values:
R R work R free
0.142 0.142 0.17
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

The role of mass spectrometry in structure elucidation of dynamic protein complexes.
Sharon et al. (2007)
2 more

7 mentions without citation

Evolution of the arginase fold and functional diversity.
Dowling et al. (2008)
6 more