3cyv

X-ray diffraction
2.8Å resolution

Crystal structure of uroporphyrinogen decarboxylase from Shigella flexineri: new insights into its catalytic mechanism

Released:
Source organism: Shigella flexneri
Entry authors: Liu H, Zhou H, Bi R

Function and Biology Details

Reaction catalysed:
Uroporphyrinogen III = coproporphyrinogen + 4 CO(2)
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Uroporphyrinogen decarboxylase Chain: A
Molecule details ›
Chain: A
Length: 354 amino acids
Theoretical weight: 39.27 KDa
Source organism: Shigella flexneri
Expression system: Escherichia coli
UniProt:
  • Canonical: Q83PB7 (Residues: 1-354; Coverage: 100%)
Gene names: S3666, SF4069, hemE
Sequence domains: Uroporphyrinogen decarboxylase (URO-D)
Structure domains: TIM Barrel

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BSRF BEAMLINE 3W1A
Spacegroup: C2221
Unit cell:
a: 68.406Å b: 136.17Å c: 77.845Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.241 0.227 0.282
Expression system: Escherichia coli