Bovine complex I in the active state at 3.1 a

Structure

electron microscopy · 45 distinct chains · 51% helix, 7% strand (DSSP).

Ligands and binding sites

• 3PE · 1,2-diacyl-sn-glycero-3-phosphoethanolamine · ligand · 13 copies · chains A, H, b, D, I, Z, J, a, K, L, M, l, h, i, N, Y, O, d, X, f, c
• SF4 · Iron/sulfur cluster · ligand · 6 copies · chains B, D, F, G, I
• PC1 · 1,2-diacyl-sn-glycero-3-phosphocholine · ligand · 5 copies · chains A, P, B, H, I, q, N, d, e, L, M, g, h
• CDL · Cardiolipin · ligand · 4 copies · chains L, M, h, N, Y, g, i, p, H, I, a, q, r
• FES · Fe2/s2 (inorganic) cluster · ligand · 2 copies · chains E, F, G
• EHZ · ~{S}-[2-[3-[[(2~{R})-3,3-dimethyl-2-oxidanyl-4-phosphonooxy-butanoyl]amino]propanoylamino]ethyl] (3~{S})-3-oxidanyltetradecanethioate · ligand · 2 copies · chains T, W, L, U, n
• FMN · Flavin mononucleotide · ligand · chains F
• GTP · Guanosine-5'-triphosphate · ligand · chains O
• NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · chains B, P
• MG · Magnesium ion · metal · chains O
• ZN · Zinc ion · metal · chains R
• LMT · Dodecyl-beta-D-maltoside · additive · 3 copies · chains L, M, N, m, D, A, H, b

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

Interfaces

202 interfaces between chains.

• A–H · 3283 Ų buried · 14 hydrogen bonds · protein-protein
• E–F · 3108 Ų buried · 32 hydrogen bonds · protein-protein
• J–K · 2917 Ų buried · 20 hydrogen bonds · protein-protein
• C–D · 2716 Ų buried · 36 hydrogen bonds · protein-protein
• L–M · 2394 Ų buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 modified, 7 disulfide, 2 covalent (disulfide, formylation, nonstandard, covalent ligand, acetylation, methylation).

Compared structures

• 7QSD · Bovine complex I in the active state at 3.1 A · the same entry in another collection · chain C against C, TM-score 1.00

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt Q7JAS9
• Every structure of UniProt P42026
• Every structure of UniProt P23709
• Every structure of UniProt P17694
• Every structure of UniProt P04394
• Every structure of UniProt P25708
• Every structure of UniProt P15690
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• Every structure of UniProt P34942
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• Every structure of UniProt O97725
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• Elsewhere: RCSB PDB 7QSD · PDBe 7QSD · UniProt Q7JAS9 · UniProt P42026 · UniProt P23709 · UniProt P17694 · UniProt P04394 · UniProt P25708 · UniProt P15690 · UniProt P03887 · UniProt P42028 · UniProt P03924 · UniProt P03902 · UniProt P03920 · UniProt P03910 · UniProt P03892 · UniProt P34942 · UniProt P34943 · UniProt Q02375 · UniProt P23934 · UniProt Q02370 · UniProt P52505 · UniProt P23935 · UniProt Q02366 · UniProt P42029 · UniProt Q8HXG6 · UniProt Q95KV7 · UniProt Q02377 · UniProt Q02371 · UniProt Q02376 · UniProt Q02827 · UniProt Q02379 · UniProt Q02378 · UniProt Q8HXG5 · UniProt Q02380 · UniProt Q02367 · UniProt Q02374 · UniProt Q02365 · UniProt Q02372 · UniProt P48305 · UniProt Q02369 · UniProt Q02368 · UniProt Q02373 · UniProt O97725 · UniProt Q05752 · UniProt P25712