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Crystal structure of GH36 alpha-galactosidase agab from geobacillus stearothermophilus

Analyse Crystal structure of GH36 alpha-galactosidase agab from geobacillus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4FNQ
Type: protein
Length: 723 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-galactosidase agab
EC: 3.2.1.22
UniProt: Q934H7
Pockets: 8 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 21% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-galactosidase agab (EC 3.2.1.22)	protein	723	21% helix, 34% strand	Q934H7

Ligands and binding sites

EDO · 1,2-ethanediol · additive · chains A

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

Pockets

8 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	57	0.71	0.98	19	empty
2	307	0.62	0.79	40	empty
3	52	0.44	0.84	17	empty
4	130	0.40	0.75	22	empty
5	139	0.39	0.73	23	empty

Compared structures

4FNQ · Crystal structure of GH36 alpha-galactosidase AgaB from Geobacillus stearothermophilus · 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 Q934H7
Elsewhere: RCSB PDB 4FNQ · PDBe 4FNQ · UniProt Q934H7

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