› 1wkv

X-ray diffraction
2Å resolution

Function and Biology Details

Reactions catalysed: 
O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
O-phospho-L-serine + hydrogen sulfide = L-cysteine + phosphate
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-195453 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein CysO Chains: A, B
Molecule details ›
Chains: A, B
Length: 389 amino acids
Theoretical weight: 42.03 KDa
Source organism: Aeropyrum pernix K1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9YBL2 (Residues: 1-389; Coverage: 100%)
Gene names: APE_1586, cysO
Sequence domains: Pyridoxal-phosphate dependent enzyme
Structure domains:

Ligands and Environments


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

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL40B2
Spacegroup: P43212
Unit cell:
a: 74.874Å b: 74.874Å c: 275.908Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.188 0.231
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Sulfur metabolism in archaea reveals novel processes.
Liu et al. (2012)
2 more

2 mentions without citation

Crystal structure of a sulfur carrier protein complex found in the cysteine biosynthetic pathway of Mycobacterium tuberculosis.
Jurgenson et al. (2008)
1 more