2ihu

X-ray diffraction
2.05Å resolution

Carboxyethylarginine synthase from Streptomyces clavuligerus: putative reaction intermediate complex

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: 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 TP8 1 x TP8
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P212121
Unit cell:
a: 119.691Å b: 127.863Å c: 197.15Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.171 0.201
Expression system: Escherichia coli BL21(DE3)