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Respiratory complex I from escherichia COLI - focused refinement of membrane arm

Analyse Respiratory complex I from escherichia COLI - focused refinement of membrane arm in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7NYH
Type
protein
Length
2,195 residues
Chains
7
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
NADH-quinone oxidoreductase subunit a; NADH-quinone oxidoreductase subunit H…
EC
7.1.1.-, 7.1.1.2, 1.6.5.11, 1.6.5.3, 1.6.99.5
UniProt
P0AFC3, P0AFD4, P0AFE0, F4VE45, A0A1V3W1N5, P0AFE8, P0AFF0
Pockets
20 · best druggability 0.83

Structure

electron microscopy · 7 distinct chains · 71% helix, 2% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ANADH-quinone oxidoreductase subunit a (EC 7.1.1.-)protein8684% helix, 0% strandP0AFC3
HNADH-quinone oxidoreductase subunit H (EC 7.1.1.-)protein26264% helix, 0% strandP0AFD4
JNADH-quinone oxidoreductase subunit J (EC 7.1.1.-)protein16476% helix, 2% strandP0AFE0
KNADH-quinone oxidoreductase subunit K (EC 7.1.1.2)protein10071% helix, 3% strandF4VE45
LNADH-quinone oxidoreductase subunit L (EC 1.6.5.11, 1.6.5.3, 1.6.99.5)protein61271% helix, 4% strandA0A1V3W1N5
MNADH-quinone oxidoreductase subunit M (EC 7.1.1.-)protein50470% helix, 2% strandP0AFE8
NNADH-quinone oxidoreductase subunit N (EC 7.1.1.-)protein46773% helix, 1% strandP0AFF0

Pockets

20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111120.830.84145empty
25680.790.8450empty
37110.770.8151empty
42480.660.8226empty
55420.660.7646empty

Interfaces

13 interfaces between chains.

  • J–K · 3267 Ų buried · 18 hydrogen bonds · protein-protein
  • L–M · 2574 Ų buried · 12 hydrogen bonds · protein-protein
  • K–N · 1776 Ų buried · 10 hydrogen bonds · protein-protein
  • M–N · 1709 Ų buried · 4 hydrogen bonds · protein-protein
  • A–H · 1661 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 7NYH · Respiratory complex I from Escherichia coli - focused refinement of membrane arm · the same entry in another collection · chain N against N, TM-score 1.00
  • P0AFF0 · AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit N (P0AFF0) · a predicted model of the same protein · chain N against A, TM-score 0.98
  • P0AFE8 · AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit M (P0AFE8) · a predicted model of the same protein · chain M against A, TM-score 0.97
  • P0AFD4 · AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit H (P0AFD4) · a predicted model of the same protein · chain H against A, TM-score 0.95
  • P0AFE0 · AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit J (P0AFE0) · a predicted model of the same protein · chain J against A, TM-score 0.90
  • P0AFC3 · AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit a (P0AFC3) · a predicted model of the same protein · chain A against A, TM-score 0.78

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