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BPGH117_H302E mutant glycoside hydrolase

Analyse BPGH117_H302E mutant glycoside hydrolase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4AK6
Type: protein
Length: 730 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Anhydro-alpha-L-galactosidase
UniProt: B5CY74
Ligands: MG
Pockets: 6 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 6% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Anhydro-alpha-L-galactosidase	protein	368	6% helix, 40% strand	B5CY74
B	Anhydro-alpha-L-galactosidase	protein	362	6% helix, 40% strand	B5CY74

Ligands and binding sites

MG · Magnesium ion · metal · 5 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	918	0.78	0.80	100	MG
2	443	0.69	0.80	32	MG
3	179	0.54	0.79	27	empty
4	152	0.51	0.79	23	empty
5	113	0.40	0.75	20	empty

Interfaces

1 interface between chains.

A–B · 3262 Å² buried · 56 hydrogen bonds · protein-protein

Compared structures

4AK6 · BpGH117_H302E mutant glycoside hydrolase · 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 B5CY74
Elsewhere: RCSB PDB 4AK6 · PDBe 4AK6 · UniProt B5CY74

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