› 2bht

X-ray diffraction
2.1Å resolution

Crystal structure of O-acetylserine sulfhydrylase B

Released:
DOI: 10.2210/pdb2bht/pdb
PDB entry 2bht coloured by chain, front view.
PDB entry 2bht coloured by chain, side view.
PDB entry 2bht coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure of the O-acetylserine sulfhydrylase isoenzyme CysM from Escherichia coli.
Claus MT, Zocher GE, Maier TH, Schulz GE
Biochemistry 44 8620-6 (2005)
PMID: 15952768

Function and Biology Details

Reaction catalysed: 
O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
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-147801 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cysteine synthase B Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 303 amino acids
Theoretical weight: 32.67 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P16703 (Residues: 1-303; Coverage: 100%)
Gene names: JW2414, b2421, cysM
Sequence domains: Pyridoxal-phosphate dependent enzyme
Structure domains: Rossmann fold

Ligands and Environments


Cofactor: Ligand PLP 4 x PLP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: I41
Unit cell:
a: 149.94Å b: 149.94Å c: 194.01Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.225 not available 0.244
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Expanding the enzyme universe: accessing non-natural reactions by mechanism-guided directed evolution.
Renata et al. (2015)
4 more

5 mentions without citation

Forcefield_PTM: Ab Initio Charge and AMBER Forcefield Parameters for Frequently Occurring Post-Translational Modifications.
Khoury et al. (2013)
4 more