MolNFT v2 · #120290 · 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: “The novel function of Osm1 under anaerobic condition in the ER was revealed by crystal structure of Osm1, a…”. X-ray diffraction at 1.8, 1 ligand (FAD). MolNFT v2 #120290 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5GLG
- Type
- protein
- Length
- 471 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.8
- Source
- Saccharomyces cerevisiae S288c
- UniProt
- P21375
- Ligands
- FAD
Structure
x-ray diffraction · resolution 1.8 · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 471 | — | P21375 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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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