MolNFT v1 · #119977 · protein
The novel function of OSM1 under anaerobic condition in the er was revealed by crystal structure of OSM1, a soluble fumarate reductase in yeast
5GLG · Fumarate reductase 2: “The novel function of OSM1 under anaerobic condition in the er was revealed by crystal structure of OSM1, a…”. X-ray diffraction, 1 ligand (FAD), 2 pockets (best druggability 0.82). MolNFT v1 #119977 on…
- PDB
- 5GLG
- Type
- protein
- Length
- 471 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fumarate reductase 2
- EC
- 1.3.1.6
- UniProt
- P21375
- Ligands
- FAD
- Pockets
- 2 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fumarate reductase 2 (EC 1.3.1.6) | protein | 471 | 34% helix, 21% strand | P21375 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 463 | 0.82 | 0.89 | 80 | SIN, FAD |
| 2 | 80 | 0.30 | 0.73 | 17 | empty |
Compared structures
- 5GLG · The novel function of Osm1 under anaerobic condition in the ER was revealed by crystal… · the same entry in another collection · chain A against A, TM-score 1.00
- P21375 · AlphaFold monomer V2.0 prediction for fumarate reductase 2 (P21375) · a predicted model of the same protein · 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 P21375
- Elsewhere: RCSB PDB 5GLG · PDBe 5GLG · UniProt P21375
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