5ijg

X-ray diffraction
2Å resolution

Crystal structure of O-acetylhomoserine sulfhydrolase from Brucella melitensis at 2.0 A resolution

Released:
Model geometry
Fit model/data
Entry authors: Boyko KM, Nikolaeva AY, Koolikova VV, Kotlov MI, Demidkina TV, Popov VO

Function and Biology Details

Reaction catalysed:
O(4)-succinyl-L-homoserine + L-cysteine = L-cystathionine + succinate
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-187066 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cystathionine gamma-synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 427 amino acids
Theoretical weight: 45.8 KDa
Source organism: Brucella melitensis bv. 1 str. 16M
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8YJI0 (Residues: 1-427; Coverage: 100%)
Gene name: BMEI0103
Sequence domains: Cys/Met metabolism PLP-dependent enzyme

Ligands and Environments


Cofactor: Ligand PLP 2 x PLP
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P3221
Unit cell:
a: 109.71Å b: 109.71Å c: 110.77Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.172 0.17 0.223
Expression system: Escherichia coli BL21(DE3)