Research workbench
Mitochondrial rhodoquinol-fumarate reductase from the parasitic nematode ascaris suum with the specific inhibitor atpenin A5
Analyse Mitochondrial rhodoquinol-fumarate reductase from the parasitic nematode… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3VRA
- Type
- protein
- Length
- 2,288 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q33862, O44074, P92506, P92507
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, E | — | protein | 613 | — | Q33862 |
| B, F | — | protein | 249 | — | O44074 |
| C, G | — | protein | 153 | — | P92506 |
| D, H | — | protein | 129 | — | P92507 |
Compared structures
- 3VRA · Mitochondrial rhodoquinol-fumarate reductase from the parasitic nematode Ascaris suum… · the same entry in another collection · chain H against H, TM-score 1.00
- 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 0.89
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 Q33862
- Every structure of UniProt O44074
- Every structure of UniProt P92506
- Every structure of UniProt P92507
- Elsewhere: RCSB PDB 3VRA · PDBe 3VRA · UniProt Q33862 · UniProt O44074 · UniProt P92506 · UniProt P92507
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