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Crystal structure of galactose oxidase, W290H mutant

Analyse Crystal structure of galactose oxidase, W290H mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2EIB
Type: protein
Length: 639 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Galactose oxidase
EC: 1.1.3.9
UniProt: Q01745
Ligands: CU, NA, SO4
Pockets: 3 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 3% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Galactose oxidase (EC 1.1.3.9)	protein	639	3% helix, 41% strand	Q01745

Ligands and binding sites

CU · Copper (II) ion · metal · chains A
NA · Sodium ion · metal · chains A
SO4 · Sulfate ion · ion · chains A
ACT · Acetate ion · additive · 3 copies · chains A

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

Pockets

3 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	60	0.57	0.90	20	empty
2	250	0.51	0.75	33	empty
3	142	0.43	0.75	25	empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

2EIB · Crystal Structure of Galactose Oxidase, W290H mutant · 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 Q01745
Elsewhere: RCSB PDB 2EIB · PDBe 2EIB · UniProt Q01745

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