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MolNFT v1 · #114899 · protein

Crystal structure of mitochondrial rhodoquinol-fumarate reductase from ascaris suum with ubiquinone-1

5C3J · Succinate dehydrogenase [ubiquinone] flavoprotein subunit…: “Crystal structure of mitochondrial rhodoquinol-fumarate reductase from ascaris suum with ubiquinone-1”. X-ray diffraction, 7 ligands (FAD, FES, SF4), 20 pockets (best…

PDB
5C3J
Type
protein
Length
2,296 residues
Chains
8
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial; Succinate…
EC
1.3.5.1
UniProt
U1LRQ3, O44074, P92506, P92507
Ligands
FAD, FES, SF4, F3S, HEM, UQ1, EPH
Pockets
20 · best druggability 0.85

Structure

x-ray diffraction · 4 distinct chains · 42% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, ESuccinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial (EC 1.3.5.1)protein61634% helix, 22% strandU1LRQ3
B, FSuccinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial (EC 1.3.5.1)protein25029% helix, 15% strandO44074
C, GCytochrome B-large subunitprotein15375% helix, 1% strandP92506
D, HSuccinate dehydrogenase [ubiquinone] cytochrome B small subunit, mitochondrialprotein12969% helix, 2% strandP92507

Ligands and binding sites

  • FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B, E, F
  • FES · Fe2/s2 (inorganic) cluster · ligand · 2 copies · chains B, F
  • SF4 · Iron/sulfur cluster · ligand · 2 copies · chains B, F
  • F3S · FE3-S4 cluster · ligand · 2 copies · chains B, F
  • HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains B, C, D, F, G, H
  • UQ1 · Ubiquinone-1 · ligand · 2 copies · chains B, C, D, F, G, H
  • EPH · L-alpha-phosphatidyl-beta-oleoyl-gamma-palmitoyl-phosphatidylethanolamine · ligand · 2 copies · chains C, D, G, H
  • MLI · Malonate ion · additive · 2 copies · chains A, 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, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111150.850.8692HEM, UQ1, EPH
22920.850.9656MLI, FAD
32670.850.9757MLI, FAD
411910.840.85102HEM, UQ1, EPH
510250.760.7888empty

Interfaces

16 interfaces between chains.

  • A–B · 2761 Ų buried · 44 hydrogen bonds · protein-protein
  • E–F · 2746 Ų buried · 42 hydrogen bonds · protein-protein
  • B–C · 1947 Ų buried · 15 hydrogen bonds · protein-protein
  • F–G · 1947 Ų buried · 17 hydrogen bonds · protein-protein
  • C–D · 1846 Ų buried · 13 hydrogen bonds · protein-protein

Compared structures

  • P92507 · AlphaFold monomer V2.0 prediction for succinate dehydrogenase [ubiquinone] cytochrome B… · a predicted model of the same protein · chain H against A, TM-score 0.90

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