1yni

X-ray diffraction
2.2Å resolution

Crystal Structure of N-Succinylarginine Dihydrolase, AstB, bound to Substrate and Product, an Enzyme from the Arginine Catabolic Pathway of Escherichia coli

Released:

Function and Biology Details

Reaction catalysed:
N(2)-succinyl-L-arginine + 2 H(2)O = N(2)-succinyl-L-ornithine + 2 NH(3) + CO(2)
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-succinylarginine dihydrolase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 458 amino acids
Theoretical weight: 50.54 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P76216 (Residues: 2-447; Coverage: 100%)
Gene names: JW1734, astB, b1745, ydjT
Sequence domains: Succinylarginine dihydrolase
Structure domains: Succinylarginine dihydrolase

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P212121
Unit cell:
a: 54.849Å b: 166.902Å c: 185.991Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.219 0.219 0.265
Expression system: Escherichia coli BL21(DE3)