Research workbench

Old yellow enzyme at 2 ångströms resolution: overall structure, ligand binding and comparison with related flavoproteins

Analyse Old yellow enzyme at 2 ångströms resolution: overall structure, ligand binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1OYA
Type: protein
Length: 399 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Old yellow enzyme
EC: 1.6.99.1
UniProt: Q02899
Ligands: FMN
Pockets: 1 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Old yellow enzyme (EC 1.6.99.1)	protein	399	37% helix, 15% strand	Q02899

Ligands and binding sites

FMN · Flavin mononucleotide · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	319	0.78	0.89	49	FMN

Compared structures

1OYA · Old yellow enzyme at 2 ångströms resolution: overall structure, ligand binding and… · the same entry in another collection · chain A against A, TM-score 1.00
Q02899 · AlphaFold monomer V2.0 prediction for NADPH dehydrogenase 1 (Q02899) · 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 Q02899
Elsewhere: RCSB PDB 1OYA · PDBe 1OYA · UniProt Q02899

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