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MolNFT v1 · #186604 · protein

Complex III2 from candida albicans, inhibitor free, rieske head domain in intermediate position

7RJC · Ubiquinol--cytochrome-C reductase subunit: “Complex III2 from candida albicans, inhibitor free, rieske head domain in intermediate position”. Electron microscopy, 4 ligands (HEM, U10, HEC), 20 pockets (best druggability 0.82).…

PDB
7RJC
Type
protein
Length
1,907 residues
Chains
10
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ubiquinol--cytochrome-C reductase subunit; Cytochrome B; Ubiquinol--cytochrome-C…
EC
7.1.1.8
UniProt
A0A1D8PP59, P0C8L0, A0A1D8PHA3, Q5ABS1, A0A1D8PHA2, A0A1D8PJT8, A0A1D8PLP3, P83782, A0A1D8PJX3
Ligands
HEM, U10, HEC, FES
Pockets
20 · best druggability 0.82

Structure

electron microscopy · 10 distinct chains · 52% helix, 10% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUbiquinol--cytochrome-C reductase subunitprotein41647% helix, 16% strandA0A1D8PP59
KCytochrome Bprotein38372% helix, 2% strandP0C8L0
DUbiquinol--cytochrome-C reductase catalytic subunitprotein24441% helix, 8% strandA0A1D8PHA3
GCytochrome B-C1 complex subunit 7protein12268% helix, 1% strandQ5ABS1
FUbiquinol--cytochrome-C reductase subunit 8protein8555% helix, 7% strandA0A1D8PHA2
HUbiquinol--cytochrome-C reductase subunit 6protein7275% helix, 0% strandA0A1D8PJT8
IUbiquinol--cytochrome-C reductase subunit 9protein3982% helix, 0% strandA0A1D8PLP3
BCytochrome B-C1 complex subunit 2, mitochondrialprotein36441% helix, 19% strandP83782
MCytochrome B-C1 complex subunit rieske, mitochondrial (EC 7.1.1.8)protein5068% helix, 0% strandA0A1D8PJX3
ECytochrome B-C1 complex subunit rieske, mitochondrial (EC 7.1.1.8)protein13215% helix, 21% strandA0A1D8PJX3

Ligands and binding sites

  • HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains K
  • U10 · Ubiquinone-10 · ligand · 2 copies · chains K
  • HEC · Heme C · ligand · chains 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, 18 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15640.820.8765HEM
24590.770.8550HEM, U10
38900.770.8086HEC
47510.750.7974empty
510720.730.76113empty

Interfaces

19 interfaces between chains.

  • K–G · 1837 Ų buried · 10 hydrogen bonds · protein-protein
  • A–B · 1796 Ų buried · 13 hydrogen bonds · protein-protein
  • K–D · 1748 Ų buried · 16 hydrogen bonds · protein-protein
  • K–F · 1376 Ų buried · 5 hydrogen bonds · protein-protein
  • D–H · 1137 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 cofactor, 1 covalent, 1 disulfide (heme c attachment, heme attachment, covalent ligand, disulfide).

Compared structures

  • 7RJC · Complex III2 from Candida albicans, inhibitor free, Rieske head domain in intermediate… · the same entry in another collection · chain E against E, TM-score 1.00
  • P0C8L0 · AlphaFold monomer V2.0 prediction for cytochrome B (P0C8L0) · a predicted model of the same protein · chain K against A, TM-score 0.99
  • P83782 · AlphaFold monomer V2.0 prediction for cytochrome B-C1 complex subunit 2, mitochondrial… · a predicted model of the same protein · chain B against A, TM-score 0.98

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