MolNFT v1 · #142252 · protein

Fumarate reductase

5ZYN · Fumarate reductase 2: “Fumarate reductase”. X-ray diffraction, 2 ligands (FMN, FAD), 3 pockets (best druggability 0.81). MolNFT v1 #142252 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5ZYN
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: FMN, FAD
Pockets: 3 · best druggability 0.81

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Fumarate reductase 2 (EC 1.3.1.6)	protein	471	34% helix, 21% strand	P21375

Ligands and binding sites

FMN · Flavin mononucleotide · ligand · chains B
FAD · Flavin-adenine dinucleotide · ligand · chains B
SIN · Succinic acid · additive · chains B

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

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	465	0.81	0.89	72	SIN, FMN, FAD
2	83	0.31	0.73	17	empty
3	59	0.29	0.74	17	empty

Compared structures

5ZYN · Fumarate reductase · the same entry in another collection · chain B against B, 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 5ZYN · PDBe 5ZYN · UniProt P21375

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