4add

X-ray diffraction
2.45Å resolution

Structural and functional study of succinyl-ornithine transaminase from E. coli

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Succinylornithine transaminase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 406 amino acids
Theoretical weight: 43.71 KDa
Source organism: Escherichia coli BL21
UniProt:
  • Canonical: P77581 (Residues: 1-406; Coverage: 100%)
Gene names: JW1737, argM, astC, b1748, cstC, ydjW
Sequence domains: Aminotransferase class-III
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 4 x PLP
1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: C2
Unit cell:
a: 183.938Å b: 118.264Å c: 109.238Å
α: 90° β: 96.82° γ: 90°
R-values:
R R work R free
0.173 0.17 0.225