MolNFT v1 · #59051 · protein

Pyranose 2-oxidase from trametes multicolor, E542K/L537W

3BLY · Pyranose oxidase: “Pyranose 2-oxidase from trametes multicolor, E542K/L537W”. X-ray diffraction, 1 ligand (FAD), 6 pockets (best druggability 0.86). MolNFT v1 #59051 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3BLY
Type: protein
Length: 573 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pyranose oxidase
EC: 1.1.3.10
UniProt: Q7ZA32
Ligands: FAD
Pockets: 6 · best druggability 0.86

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Pyranose oxidase (EC 1.1.3.10)	protein	573	26% helix, 23% strand	Q7ZA32

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · chains A
MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	777	0.86	0.89	77	FAD
2	308	0.65	0.81	35	empty
3	103	0.61	0.87	25	empty
4	51	0.34	0.79	17	empty
5	76	0.34	0.75	12	empty

Modifications

Observed in the structure: 1 cofactor (flavinylation).

Compared structures

3BLY · Pyranose 2-oxidase from Trametes multicolor, E542K/L537W · the same entry in another collection · 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 Q7ZA32
Elsewhere: RCSB PDB 3BLY · PDBe 3BLY · UniProt Q7ZA32

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