› 1gn9

X-ray diffraction
2.6Å resolution

Hybrid Cluster Protein from Desulfovibrio desulfuricans ATCC 27774 X-ray structure at 2.6A resolution using synchrotron radiation at a wavelength of 1.722A

Released:
DOI: 10.2210/pdb1gn9/pdb
PDB entry 1gn9 coloured by chain, front view.
PDB entry 1gn9 coloured by chain, side view.
PDB entry 1gn9 coloured by chain, top view.
Source organism: Desulfovibrio desulfuricans
Primary publication:
Hybrid cluster proteins (HCPs) from Desulfovibrio desulfuricans ATCC 27774 and Desulfovibrio vulgaris (Hildenborough): X-ray structures at 1.25 A resolution using synchrotron radiation.
Macedo S, Mitchell EP, Romão CV, Cooper SJ, Coelho R, Liu MY, Xavier AV, LeGall J, Bailey S, Garner DC, Hagen WR, Teixeira M, Carrondo MA, Lindley P
J Biol Inorg Chem 7 514-25 (2002)
PMID: 11941509

Function and Biology Details

Reaction catalysed: 
NH(3) + H(2)O + acceptor = hydroxylamine + reduced acceptor
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169625 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hydroxylamine reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 544 amino acids
Theoretical weight: 58.63 KDa
Source organism: Desulfovibrio desulfuricans
UniProt:
  • Canonical: Q01770 (Residues: 2-545; Coverage: 100%)
Gene names: Ddes_1829, hcp
Sequence domains: Prismane/CO dehydrogenase family
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand FSO 2 x FSO
Ligand SF4 2 x SF4
1 modified residue:
Ligand CSS 2 x CSS

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P1
Unit cell:
a: 57.4Å b: 61.8Å c: 72.2Å
α: 82.7° β: 73.7° γ: 87.3°
R-values:
R R work R free
0.193 0.193 0.26

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Citations

1 review citation

Molecular understanding of heteronuclear active sites in heme-copper oxidases, nitric oxide reductases, and sulfite reductases through biomimetic modelling.
Reed et al. (2021)
11 other articles