› 4he8

X-ray diffraction
3.3Å resolution

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

Released:
DOI: 10.2210/pdb4he8/pdb
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PDB entry 4he8 coloured by chain, front view.
PDB entry 4he8 coloured by chain, side view.
PDB entry 4he8 coloured by chain, top view.
Source organism: Thermus thermophilus HB8
Primary publication:
Crystal structure of the entire respiratory complex I.
Baradaran R, Berrisford JM, Minhas GS, Sazanov LA
OpenAccess logo Nature 494 443-8 (2013)
PMID: 23417064

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero heptamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176330 (preferred)
Entry contents:
7 distinct polypeptide molecules
Macromolecules (7 distinct):
NADH-quinone oxidoreductase subunit 7 Chains: A, B
Molecule details ›
Chains: A, B
Length: 119 amino acids
Theoretical weight: 13.15 KDa
Source organism: Thermus thermophilus HB8
UniProt:
  • Canonical: Q56217 (Residues: 1-119; Coverage: 100%)
Gene names: TTHA0084, nqo7
Sequence domains: NADH-ubiquinone/plastoquinone oxidoreductase, chain 3
Structure domains: NADH:ubiquinone/plastoquinone oxidoreductase, chain 3
NADH-quinone oxidoreductase subunit 10 Chains: D, J
Molecule details ›
Chains: D, J
Length: 176 amino acids
Theoretical weight: 18.56 KDa
Source organism: Thermus thermophilus HB8
UniProt:
  • Canonical: Q56225 (Residues: 1-176; Coverage: 100%)
Gene names: TTHA0093, nqo10
Sequence domains: NADH-ubiquinone/plastoquinone oxidoreductase chain 6
Structure domains: NADH-ubiquinone/plastoquinone oxidoreductase chain 6, subunit NuoJ
NADH-quinone oxidoreductase subunit 11 Chains: E, K
NADH-quinone oxidoreductase subunit 12 Chains: F, L
NADH-quinone oxidoreductase subunit 13 Chains: G, M
NADH-quinone oxidoreductase subunit 14 Chains: I, N
NADH-quinone oxidoreductase subunit 8 Chains: C, H

Ligands and Environments

1 bound ligand:
Ligand UMQ 4 x UMQ
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P1
Unit cell:
a: 85.26Å b: 120.54Å c: 176.66Å
α: 91.91° β: 95.73° γ: 101.41°
R-values:
R R work R free
0.21 0.209 0.263

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Citations

103 review citations

Mitochondrial generation of superoxide and hydrogen peroxide as the source of mitochondrial redox signaling.
Brand MD. (2016)
102 more

12 mentions without citation

Structural Symmetry in Membrane Proteins.
Forrest LR. (2015)
11 more

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