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Pyranose 2-oxidase H450G mutant with 2-fluorinated galactose

Analyse Pyranose 2-oxidase H450G mutant with 2-fluorinated galactose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4MOO
Type: protein
Length: 576 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pyranose 2-oxidase
EC: 1.1.3.10
UniProt: Q7ZA32
Ligands: FDA, GAF
Pockets: 4 · best druggability 0.88

Structure

x-ray diffraction · 1 distinct chain · 24% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Pyranose 2-oxidase (EC 1.1.3.10)	protein	576	24% helix, 23% strand	Q7ZA32

Ligands and binding sites

FDA · Dihydroflavine-adenine dinucleotide · ligand · chains A
GAF · 2-deoxy-2-fluoro-alpha-D-galactopyranose · ligand · 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, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	493	0.88	0.95	65	FDA, GAF
2	434	0.73	0.83	57	empty
3	96	0.51	0.82	24	empty
4	89	0.35	0.74	12	empty

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

4MOO · Pyranose 2-oxidase H450G mutant with 2-fluorinated galactose · 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 4MOO · PDBe 4MOO · UniProt Q7ZA32

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