Research workbench

OSM1 mutant - R326A

Analyse OSM1 mutant - R326A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6KU6
Type: protein
Length: 942 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P21375
Ligands: FAD

Structure

x-ray diffraction · 1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, H	—	protein	471	—	P21375

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains B, H
SIN · Succinic acid · additive · 2 copies · chains B, H

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

6KU6 · OSM1 mutant - R326A · the same entry in another collection · chain H against H, TM-score 1.00
P21375 · AlphaFold monomer V2.0 prediction for fumarate reductase 2 (P21375) · a predicted model of the same protein · chain B 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 6KU6 · PDBe 6KU6 · UniProt P21375

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