› 2gep

X-ray diffraction
1.9Å resolution

SULFITE REDUCTASE HEMOPROTEIN, OXIDIZED, SIROHEME FEIII [4FE-4S] +2,SULFITE COMPLEX

Released:
DOI: 10.2210/pdb2gep/pdb
PDB entry 2gep coloured by chain, front view.
PDB entry 2gep coloured by chain, side view.
PDB entry 2gep coloured by chain, top view.
Source organism: Escherichia coli B
Primary publication:
Probing the catalytic mechanism of sulfite reductase by X-ray crystallography: structures of the Escherichia coli hemoprotein in complex with substrates, inhibitors, intermediates, and products.
Crane BR, Siegel LM, Getzoff ED
Biochemistry 36 12120-37 (1997)
PMID: 9315849

Function and Biology Details

Reaction catalysed: 
H(2)S + 3 NADP(+) + 3 H(2)O = sulfite + 3 NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148188 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sulfite reductase [NADPH] hemoprotein beta-component Chain: A
Molecule details ›
Chain: A
Length: 497 amino acids
Theoretical weight: 55.75 KDa
Source organism: Escherichia coli B
Expression system: Salmonella enterica subsp. enterica serovar Typhimurium
UniProt:
  • Canonical: P17846 (Residues: 74-570; Coverage: 87%)
Gene names: JW2733, b2763, cysI
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand SRM 1 x SRM
3 bound ligands:
Ligand SO3 1 x SO3
Ligand NA 1 x NA
Ligand SF4 1 x SF4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P212121
Unit cell:
a: 69.8Å b: 77.4Å c: 87.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.175 not available
Expression system: Salmonella enterica subsp. enterica serovar Typhimurium

Quick links

Citations

12 review citations

Proton-coupled electron transfer.
Huynh et al. (2007)
11 more

4 mentions without citation

Artificial Metalloenzymes: Challenges and Opportunities.
Davis et al. (2019)
3 more