› 1upb

X-ray diffraction
2.35Å resolution

Carboxyethylarginine synthase from Streptomyces clavuligerus

Released:
DOI: 10.2210/pdb1upb/pdb
PDB entry 1upb coloured by chain, front view.
PDB entry 1upb coloured by chain, side view.
PDB entry 1upb coloured by chain, top view.
Source organism: Streptomyces clavuligerus
Primary publication:
Crystal structure and mechanistic implications of N2-(2-carboxyethyl)arginine synthase, the first enzyme in the clavulanic acid biosynthesis pathway.
Caines ME, Elkins JM, Hewitson KS, Schofield CJ
J Biol Chem 279 5685-92 (2004)
PMID: 14623876

Function and Biology Details

Reaction catalysed: 
D-glyceraldehyde 3-phosphate + L-arginine = N(2)-(2-carboxyethyl)-L-arginine + phosphate
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-192261 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N(2)-(2-carboxyethyl)arginine synthase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 573 amino acids
Theoretical weight: 60.96 KDa
Source organism: Streptomyces clavuligerus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9LCV9 (Residues: 1-573; Coverage: 100%)
Gene name: ceaS
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand TPP 4 x TPP
2 bound ligands:
Ligand MG 4 x MG
Ligand SO4 8 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX14.1
Spacegroup: P212121
Unit cell:
a: 117.703Å b: 127.276Å c: 197.091Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.159 0.157 0.196
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

The enzymes of β-lactam biosynthesis.
Hamed et al. (2013)
5 more

2 mentions without citation

Recent advances in design of new urease inhibitors: A review.
Kafarski et al. (2018)
1 more