› 4g38

X-ray diffraction
1.56Å resolution

Mutational analysis of sulfite reductase hemoprotein reveals the mechanism for coordinated electron and proton transfer

Released:
DOI: 10.2210/pdb4g38/pdb
PDB entry 4g38 coloured by chain, front view.
PDB entry 4g38 coloured by chain, side view.
PDB entry 4g38 coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Mutational analysis of sulfite reductase hemoprotein reveals the mechanism for coordinated electron and proton transfer.
Smith KW, Stroupe ME
Biochemistry 51 9857-68 (2012)
PMID: 23153334

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 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: 570 amino acids
Theoretical weight: 64.16 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P17846 (Residues: 1-570; Coverage: 100%)
Gene names: JW2733, b2763, cysI
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand SRM 1 x SRM
3 bound ligands:
Ligand PO4 1 x PO4
Ligand K 1 x K
Ligand SF4 1 x SF4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: P212121
Unit cell:
a: 66.327Å b: 76.171Å c: 81.463Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.141 0.14 0.178
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Biochemistry and theory of proton-coupled electron transfer.
Migliore et al. (2014)
1 more