› 2fug

X-ray diffraction
3.3Å resolution

Crystal structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus

Released:
DOI: 10.2210/pdb2fug/pdb
Model geometry
Fit model/data
PDB entry 2fug coloured by chain, front view.
PDB entry 2fug coloured by chain, side view.
PDB entry 2fug coloured by chain, top view.
Source organism: Thermus thermophilus HB8
Primary publication:
Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus.
Sazanov LA, Hinchliffe P
Science 311 1430-6 (2006)
PMID: 16469879

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176331 (preferred)
Entry contents:
8 distinct polypeptide molecules
Macromolecules (8 distinct):
NADH-quinone oxidoreductase subunit 1 Chains: 1, A, J, S
Molecule details ›
Chains: 1, A, J, S
Length: 438 amino acids
Theoretical weight: 48.69 KDa
Source organism: Thermus thermophilus HB8
UniProt:
  • Canonical: Q56222 (Residues: 1-438; Coverage: 100%)
Gene names: TTHA0089, nqo1
Sequence domains:
Structure domains:
NADH-quinone oxidoreductase subunit 2 Chains: 2, B, K, T
Molecule details ›
Chains: 2, B, K, T
Length: 181 amino acids
Theoretical weight: 20.31 KDa
Source organism: Thermus thermophilus HB8
UniProt:
  • Canonical: Q56221 (Residues: 1-181; Coverage: 100%)
Gene names: TTHA0088, nqo2
Sequence domains: Thioredoxin-like [2Fe-2S] ferredoxin
Structure domains:
NADH-quinone oxidoreductase subunit 3 Chains: 3, C, L, U
NADH-quinone oxidoreductase subunit 4 Chains: 4, D, M, V
NADH-quinone oxidoreductase subunit 5 Chains: 5, E, N, W
NADH-quinone oxidoreductase subunit 6 Chains: 6, F, O, X
NADH-quinone oxidoreductase subunit 9 Chains: 9, G, P, Y
NADH-quinone oxidoreductase subunit 15 Chains: 7, H, Q, Z

Ligands and Environments

3 bound ligands:
Ligand SF4 28 x SF4
Ligand FES 8 x FES
Ligand FMN 4 x FMN
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P21
Unit cell:
a: 135.08Å b: 266.112Å c: 201.731Å
α: 90° β: 104.71° γ: 90°
R-values:
R R work R free
0.265 0.265 0.298

Quick links

Citations

115 review citations

How mitochondria produce reactive oxygen species.
Murphy MP. (2009)
114 more

34 mentions without citation

Protein co-evolution, co-adaptation and interactions.
Pazos et al. (2008)
33 more