› 5xcp

X-ray diffraction
2.04Å resolution

Crystal structure of M92A mutant of O-acetyl-L-serine sulfhydrylase from Haemophilus influenzae

Released:
DOI: 10.2210/pdb5xcp/pdb
PDB entry 5xcp coloured by chain, front view.
PDB entry 5xcp coloured by chain, side view.
PDB entry 5xcp coloured by chain, top view.
Source organism: Haemophilus influenzae Rd KW20
Primary publication:
Molecular mechanism of selective substrate engagement and inhibitor disengagement of cysteine synthase.
Kaushik A, Rahisuddin R, Saini N, Singh RP, Kaur R, Koul S, Kumaran S
OpenAccess logo J Biol Chem 296 100041
PMID: 33162395

Function and Biology Details

Reaction catalysed: 
O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155240 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cysteine synthase Chain: X
Molecule details ›
Chain: X
Length: 350 amino acids
Theoretical weight: 37.14 KDa
Source organism: Haemophilus influenzae Rd KW20
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
  • Canonical: P45040 (Residues: 1-316; Coverage: 100%)
Gene names: HI_1103, cysK
Sequence domains: Pyridoxal-phosphate dependent enzyme
Structure domains: Rossmann fold

Ligands and Environments

No bound ligands
1 modified residue:
Ligand LLP 1 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: I41
Unit cell:
a: 112.39Å b: 112.39Å c: 45.63Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.152 0.151 0.168
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'

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Citations

1 review citation

Structural Basis for Allostery in PLP-dependent Enzymes.
Tran et al. (2022)

2 mentions without citation

Insights into multifaceted activities of CysK for therapeutic interventions.
Joshi et al. (2019)
1 more