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Crystal structure of mitochondrial cytochrome BC1 complex at 2.4 ångström

Analyse Crystal structure of mitochondrial cytochrome BC1 complex at 2.4 ångström in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1NTM
Type
protein
Length
2,099 residues
Chains
11
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ubiquinol-cytochrome C reductase complex core protein I, mitochondrial…
EC
1.10.2.2
UniProt
P31800, P23004, P00157, P00125, P13272, P00129, P13271, P00126, P00130, P07552
Ligands
HEM, FES
Pockets
20 · best druggability 0.86

Structure

x-ray diffraction · 11 distinct chains · 51% helix, 12% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUbiquinol-cytochrome C reductase complex core protein I, mitochondrial (EC 1.10.2.2)protein44646% helix, 19% strandP31800
BUbiquinol-cytochrome C reductase complex core protein 2, mitochondrial (EC 1.10.2.2)protein42344% helix, 20% strandP23004
CCytochrome Bprotein37873% helix, 2% strandP00157
DCytochrome C1protein24141% helix, 3% strandP00125
EUbiquinol-cytochrome C reductase iron-sulfur subunit, mitochondrial (EC 1.10.2.2)protein19630% helix, 22% strandP13272
FUbiquinol-cytochrome C reductase complex 14 kda protein (EC 1.10.2.2)protein10570% helix, 0% strandP00129
GUbiquinol-cytochrome C reductase complex ubiquinone-binding protein qp-C (EC 1.10.2.2)protein7549% helix, 12% strandP13271
HUbiquinol-cytochrome C reductase complex 11 kda protein (EC 1.10.2.2)protein6769% helix, 0% strandP00126
IUbiquinol-cytochrome C reductase 8 kda protein (EC 1.10.2.2)protein575% helix, 11% strandP13272
JUbiquinol-cytochrome C reductase complex 7.2 kda protein (EC 1.10.2.2)protein6077% helix, 0% strandP00130
KUbiquinol-cytochrome C reductase complex 6.4 kda protein (EC 1.10.2.2)protein5171% helix, 0% strandP07552

Ligands and binding sites

  • HEM · Protoporphyrin IX containing Fe · ligand · 3 copies · chains C, D
  • FES · Fe2/s2 (inorganic) cluster · ligand · chains E

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

Pockets

20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14680.860.9353HEM
28560.820.8592empty
37030.810.8565empty
411900.800.81100empty
54970.800.8650HEM

Interfaces

24 interfaces between chains.

  • A–B · 2243 Ų buried · 39 hydrogen bonds · protein-protein
  • B–I · 2033 Ų buried · 21 hydrogen bonds · protein-protein
  • C–D · 1676 Ų buried · 14 hydrogen bonds · protein-protein
  • A–I · 1441 Ų buried · 26 hydrogen bonds · protein-protein
  • C–F · 1232 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 1NTM · Crystal Structure of Mitochondrial Cytochrome bc1 Complex at 2.4 Angstrom · the same entry in another collection · chain K against K, TM-score 1.00
  • P00157 · AlphaFold monomer V2.0 prediction for cytochrome B (P00157) · a predicted model of the same protein · chain C against A, TM-score 1.00

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