Research workbench
Crystal structure of MENAQUINOL:FUMARATE oxidoreductase in complex with fumarate
Analyse Crystal structure of MENAQUINOL:FUMARATE oxidoreductase in complex with fumarate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3P4P
- Type
- protein
- Length
- 2,138 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fumarate reductase flavoprotein subunit; Fumarate reductase iron-sulfur protein; Fumarate…
- EC
- 1.3.99.1
- UniProt
- D3GV56, Q0T9N6, C9QU46, C9QU47
- Ligands
- FAD, FES, F3S, SF4, FUM
- Pockets
- 20 · best druggability 0.84
Structure
x-ray diffraction · 4 distinct chains · 47% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, M | Fumarate reductase flavoprotein subunit (EC 1.3.99.1) | protein | 577 | 40% helix, 20% strand | D3GV56 |
| B, N | Fumarate reductase iron-sulfur protein (EC 1.3.99.1) | protein | 243 | 40% helix, 14% strand | Q0T9N6 |
| C, O | Fumarate reductase subunit C | protein | 130 | 74% helix, 4% strand | C9QU46 |
| D, P | Fumarate reductase subunit D | protein | 119 | 71% helix, 0% strand | C9QU47 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, M
- FES · Fe2/s2 (inorganic) cluster · ligand · 2 copies · chains B, N
- F3S · FE3-S4 cluster · ligand · 2 copies · chains B, N
- SF4 · Iron/sulfur cluster · ligand · 2 copies · chains B, N
- FUM · Fumaric acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 288 | 0.84 | 0.95 | 50 | FAD |
| 2 | 550 | 0.82 | 0.88 | 83 | FAD, FUM |
| 3 | 1064 | 0.82 | 0.83 | 111 | empty |
| 4 | 136 | 0.80 | 0.97 | 34 | empty |
| 5 | 730 | 0.79 | 0.83 | 60 | empty |
Interfaces
13 interfaces between chains.
- M–N · 2720 Ų buried · 53 hydrogen bonds · protein-protein
- A–B · 2681 Ų buried · 40 hydrogen bonds · protein-protein
- C–D · 2359 Ų buried · 15 hydrogen bonds · protein-protein
- O–P · 2292 Ų buried · 15 hydrogen bonds · protein-protein
- N–O · 1465 Ų buried · 20 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 cofactor (flavinylation).
Compared structures
- 3P4P · Crystal structure of Menaquinol:fumarate oxidoreductase in complex with fumarate · the same entry in another collection · chain A against A, 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 D3GV56
- Every structure of UniProt Q0T9N6
- Every structure of UniProt C9QU46
- Every structure of UniProt C9QU47
- Elsewhere: RCSB PDB 3P4P · PDBe 3P4P · UniProt D3GV56 · UniProt Q0T9N6 · UniProt C9QU46 · UniProt C9QU47
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.