› 5n1t

X-ray diffraction
2.6Å resolution

Crystal structure of complex between flavocytochrome c and copper chaperone CopC from T. paradoxus

Released:
DOI: 10.2210/pdb5n1t/pdb
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PDB entry 5n1t coloured by chain, front view.
PDB entry 5n1t coloured by chain, side view.
PDB entry 5n1t coloured by chain, top view.
Source organism: Thioalkalivibrio paradoxus ARh 1
Primary publication:
Structure of the flavocytochrome c sulfide dehydrogenase associated with the copper-binding protein CopC from the haloalkaliphilic sulfur-oxidizing bacterium Thioalkalivibrio paradoxusARh 1.
Osipov EM, Lilina AV, Tsallagov SI, Safonova TN, Sorokin DY, Tikhonova TV, Popov VO
Acta Crystallogr D Struct Biol 74 632-642 (2018)
PMID: 29968673

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-197701 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Cytochrome C Chain: A
Molecule details ›
Chain: A
Length: 429 amino acids
Theoretical weight: 46.26 KDa
Source organism: Thioalkalivibrio paradoxus ARh 1
UniProt:
  • Canonical: W0DP88 (Residues: 1-429; Coverage: 100%)
Gene name: THITH_13285
Sequence domains:
Structure domains:
Cytochrome c domain-containing protein Chain: B
Molecule details ›
Chain: B
Length: 102 amino acids
Theoretical weight: 10.63 KDa
Source organism: Thioalkalivibrio paradoxus ARh 1
UniProt:
  • Canonical: W0DKT4 (Residues: 1-102; Coverage: 100%)
Gene name: THITH_13280
Sequence domains: Cytochrome c
Structure domains: Cytochrome c-like domain
CopC domain-containing protein Chains: M, W

Ligands and Environments

4 bound ligands:
Ligand FAD 1 x FAD
Ligand HEC 1 x HEC
Ligand CU 1 x CU
Ligand GOL 1 x GOL
1 modified residue:
Ligand CSS 1 x CSS

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P212121
Unit cell:
a: 39.53Å b: 138.4Å c: 155.81Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.186 0.257

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Citations

2 citation in other articles

The copper-linked Escherichia coli AZY operon: Structure, metal binding, and a possible physiological role in copper delivery.
Hadley et al. (2022)
1 more

4 mentions without citation

Biochemical evidence of both copper chelation and oxygenase activity at the histidine brace.
Brander et al. (2020)
3 more

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