› 1m54

X-ray diffraction
2.9Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152934 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cystathionine beta-synthase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 363 amino acids
Theoretical weight: 39.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P35520 (Residues: 44-406; Coverage: 66%)
Gene name: CBS
Sequence domains: Pyridoxal-phosphate dependent enzyme
Structure domains: Rossmann fold

Ligands and Environments


Cofactor: Ligand PLP 6 x PLP

Cofactor: Ligand HEM 6 x HEM
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-D
Spacegroup: P1
Unit cell:
a: 85.74Å b: 85.626Å c: 97.082Å
α: 102.01° β: 101.53° γ: 112.6°
R-values:
R R work R free
0.271 0.271 0.365
Expression system: Escherichia coli BL21

Quick links

Citations

20 review citations

Sulfur amino acid metabolism: pathways for production and removal of homocysteine and cysteine.
Stipanuk MH. (2004)
19 more

18 mentions without citation

Hydrogen sulfide and hemeproteins: knowledge and mysteries.
Pietri et al. (2011)
17 more