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The novel function of Osm1 under anaerobic condition in the ER was revealed by crystal structure of Osm1, a soluble fumarate reductase in yeast

Analyse The novel function of Osm1 under anaerobic condition in the ER was revealed by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

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
Molecule
Fumarate reductase 2
EC
1.3.1.6
UniProt
P21375
Ligands
FAD
Pockets
2 · best druggability 0.82

Structure

x-ray diffraction · resolution 1.8 · 1 distinct chain · 34% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFumarate reductase 2 (EC 1.3.1.6)protein47134% helix, 21% strandP21375

Ligands and binding sites

  • FAD · Flavin-adenine dinucleotide · ligand · chains A
  • SIN · Succinic acid · additive · chains A

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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14630.820.8980SIN, FAD
2800.300.7317empty

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

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