Research workbench

Glucose-fructose oxidoreductase

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

PDB: 1OFG
Type: protein
Length: 2,286 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glucose-fructose oxidoreductase
EC: 1.1.99.28
UniProt: Q07982
Ligands: NDP
Pockets: 20 · best druggability 0.87

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F	Glucose-fructose oxidoreductase (EC 1.1.99.28)	protein	381	36% helix, 22% strand	Q07982

Ligands and binding sites

NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · 6 copies · chains A, D, B, C, E, F

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

Pockets

20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1006	0.87	0.88	98	empty
2	1073	0.85	0.86	83	empty
3	1063	0.85	0.86	81	empty
4	543	0.84	0.89	74	NDP
5	547	0.83	0.89	72	NDP

Interfaces

7 interfaces between chains.

A–D · 3309 Å² buried · 38 hydrogen bonds · protein-protein
B–C · 3303 Å² buried · 37 hydrogen bonds · protein-protein
C–D · 1678 Å² buried · 30 hydrogen bonds · protein-protein
A–B · 1678 Å² buried · 31 hydrogen bonds · protein-protein
E–F · 1676 Å² buried · 31 hydrogen bonds · protein-protein

Compared structures

1OFG · Glucose-fructose oxidoreductase · the same entry in another collection · chain F against F, TM-score 1.00
Q07982 · AlphaFold monomer V2.0 prediction for glucose--fructose oxidoreductase (Q07982) · 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 Q07982
Elsewhere: RCSB PDB 1OFG · PDBe 1OFG · UniProt Q07982

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