› 1gkr

X-ray diffraction
2.6Å resolution

L-Hydantoinase (Dihydropyrimidinase) from Arthrobacter aurescens

Released:
DOI: 10.2210/pdb1gkr/pdb
PDB entry 1gkr coloured by chain, front view.
PDB entry 1gkr coloured by chain, side view.
PDB entry 1gkr coloured by chain, top view.
Source organism: Paenarthrobacter aurescens
Primary publication:
The structure of L-hydantoinase from Arthobacter aurescens leads to an understanding of dihydropyrimidinase substrate and enantio specificity.
Abendroth J, Niefind K, May O, Siemann M, Syldatk C, Schomburg D
Biochemistry 41 8589-97 (2002)
PMID: 12093275

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160467 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-hydantoinase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 458 amino acids
Theoretical weight: 49.69 KDa
Source organism: Paenarthrobacter aurescens
UniProt:
  • Canonical: P81006 (Residues: 1-458; Coverage: 100%)
Gene name: lhyD
Sequence domains: Amidohydrolase family
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ZN 8 x ZN
1 modified residue:
Ligand KCX 4 x KCX

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 111.5Å b: 74.3Å c: 146.9Å
α: 90° β: 106.57° γ: 90°
R-values:
R R work R free
0.224 0.224 0.244

Quick links

Citations

5 review citations

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

5 mentions without citation

Structural bases for CRMP function in plexin-dependent semaphorin3A signaling.
Deo et al. (2004)
4 more