2iht

X-ray diffraction
2Å resolution

Carboxyethylarginine synthase from Streptomyces clavuligerus: SeMet structure

Released:
Source organism: Streptomyces clavuligerus
Primary publication:
Structural and mechanistic studies on N(2)-(2-carboxyethyl)arginine synthase.
Biochem Biophys Res Commun 385 512-7 (2009)
PMID: 19477162

Function and Biology Details

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
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: 61.48 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
3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX14.1
Spacegroup: P212121
Unit cell:
a: 117.882Å b: 127.279Å c: 197.328Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.154 0.154 0.178
Expression system: Escherichia coli BL21(DE3)