› 5ohx

X-ray diffraction
3.2Å resolution

Structure of active cystathionine B-synthase from Apis mellifera

Released:
DOI: 10.2210/pdb5ohx/pdb
PDB entry 5ohx coloured by chain, front view.
PDB entry 5ohx coloured by chain, side view.
PDB entry 5ohx coloured by chain, top view.
Source organism: Apis mellifera
Primary publication:
Crystal structure of cystathionine β-synthase from honeybee Apis mellifera.
Giménez-Mascarell P, Majtan T, Oyenarte I, Ereño-Orbea J, Majtan J, Klaudiny J, Kraus JP, Martínez-Cruz LA
J Struct Biol 202 82-93 (2018)
PMID: 29275181

Function and Biology Details

Reaction catalysed: 
L-serine + L-homocysteine = L-cystathionine + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174084 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cystathionine beta-synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 504 amino acids
Theoretical weight: 56.29 KDa
Source organism: Apis mellifera
Expression system: Escherichia coli
UniProt:
  • Canonical: Q2V0C9 (Residues: 1-504; Coverage: 100%)
Gene name: CBS
Sequence domains: Pyridoxal-phosphate dependent enzyme
Structure domains: Rossmann fold

Ligands and Environments


Cofactor: Ligand PLP 2 x PLP

Cofactor: Ligand HEM 2 x HEM
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR-H
Spacegroup: P212121
Unit cell:
a: 86.143Å b: 96.099Å c: 180.684Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.197 0.231
Expression system: Escherichia coli

Quick links

Citations

5 citation in other articles

Cystathionine β-synthase is involved in cysteine biosynthesis and H2S generation in Toxoplasma gondii.
Conter et al. (2020)
4 more

1 mention without citation

Insights into Domain Organization and Regulatory Mechanism of Cystathionine Beta-Synthase from Toxoplasma gondii.
Conter et al. (2022)