› 1ft5

X-ray diffraction
1.6Å resolution

CRYSTAL STRUCTURE OF THE OXIDIZED STATE OF CYTOCHROME C554 FROM NITROSOMONAS EUROPAEA

Released:
DOI: 10.2210/pdb1ft5/pdb
Model geometry
Fit model/data
Data not deposited
PDB entry 1ft5 coloured by chain, front view.
PDB entry 1ft5 coloured by chain, side view.
PDB entry 1ft5 coloured by chain, top view.
Source organism: Nitrosomonas europaea
Primary publication:
High-resolution structures of the oxidized and reduced states of cytochrome c554 from Nitrosomonas europaea.
Iverson TM, Arciero DM, Hooper AB, Rees DC
J Biol Inorg Chem 6 390-7 (2001)
PMID: 11372197

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176404 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome c-554 Chain: A
Molecule details ›
Chain: A
Length: 211 amino acids
Theoretical weight: 23.66 KDa
Source organism: Nitrosomonas europaea
UniProt:
  • Canonical: Q57142 (Residues: 25-235; Coverage: 100%)
Gene names: NE0960, NE2042, NE2337, cycA, cycA1, cycA2, cycA3, hcy
Sequence domains: Cytochrome c554 and c-prime
Structure domains: Flavocytochrome C3; Chain A

Ligands and Environments

2 bound ligands:
Ligand PO4 3 x PO4
Ligand HEM 4 x HEM
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: R3
Unit cell:
a: 147.892Å b: 147.892Å c: 33.913Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.188 0.188 0.215

Quick links

Citations

7 review citations

Metabolism of inorganic N compounds by ammonia-oxidizing bacteria.
Arp et al. (2003)
6 more

2 mentions without citation

How Thermophilic Gram-Positive Organisms Perform Extracellular Electron Transfer: Characterization of the Cell Surface Terminal Reductase OcwA.
Costa et al. (2019)
1 more