1xpy

X-ray diffraction
2.3Å resolution

Structural Basis for Catalytic Racemization and Substrate Specificity of an N-Acylamino Acid Racemase Homologue from Deinococcus radiodurans

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
o-succinylbenzoate synthase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 375 amino acids
Theoretical weight: 41.06 KDa
Source organism: Deinococcus radiodurans
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9RYA6 (Residues: 1-375; Coverage: 100%)
Gene names: DR_0044, menC
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL12B2
Spacegroup: P4
Unit cell:
a: 116.159Å b: 116.159Å c: 120.426Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.171 0.227
Expression system: Escherichia coli