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Pyranose 2-oxidase thermostable triple mutant, T169G/E542K/V546C

Analyse Pyranose 2-oxidase thermostable triple mutant, T169G/E542K/V546C in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3FDY
Type: protein
Length: 576 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pyranose oxidase (pyranose 2-oxidase)
EC: 1.1.3.10
UniProt: Q7ZA32
Ligands: FAD
Pockets: 4 · best druggability 0.86

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Pyranose oxidase (pyranose 2-oxidase) (EC 1.1.3.10)	protein	576	25% 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

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1059	0.86	0.87	102	FAD
2	90	0.54	0.84	23	empty
3	86	0.34	0.74	13	empty
4	58	0.29	0.74	21	empty

Modifications

Observed in the structure: 1 cofactor (flavinylation).

Compared structures

3FDY · Pyranose 2-oxidase thermostable triple mutant, T169G/E542K/V546C · 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 3FDY · PDBe 3FDY · UniProt Q7ZA32

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