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Family GH13_31 enzyme

Analyse Family GH13_31 enzyme in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6Y9T
Type: protein
Length: 1,071 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-glucosidase
UniProt: A0A3A9XV51
Ligands: CA
Pockets: 14 · best druggability 0.66

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-glucosidase	protein	536	34% helix, 17% strand	A0A3A9XV51
B	Alpha-glucosidase	protein	535	34% helix, 17% strand	A0A3A9XV51

Ligands and binding sites

CA · Calcium ion · metal · 2 copies · chains A, B

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

Pockets

14 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	423	0.66	0.79	56	empty
2	329	0.64	0.80	49	empty
3	78	0.53	0.84	16	empty
4	68	0.50	0.85	21	empty
5	122	0.49	0.80	35	empty

Interfaces

1 interface between chains.

A–B · 1880 Å² buried · 23 hydrogen bonds · protein-protein

Compared structures

6Y9T · Family GH13_31 enzyme · 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 A0A3A9XV51
Elsewhere: RCSB PDB 6Y9T · PDBe 6Y9T · UniProt A0A3A9XV51

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