MolNFT v1 · #72159 · protein

The crystal structure of the alpha-glucosidase (family 31) from ruminococcus obeum atcc 29174

3N04: “The crystal structure of the alpha-glucosidase (family 31) from ruminococcus obeum atcc 29174”. X-ray diffraction, 12 pockets (best druggability 0.86). MolNFT v1 #72159 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3N04
Type: protein
Length: 1,328 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-glucosidase
UniProt: A5ZY13
Pockets: 12 · best druggability 0.86

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Alpha-glucosidase	protein	664	28% helix, 27% strand	A5ZY13

Ligands and binding sites

GOL · Glycerol · additive · 3 copies · chains A, B

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

Pockets

12 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1134	0.86	0.87	117	empty
2	425	0.75	0.84	55	GOL
3	465	0.74	0.83	59	GOL
4	224	0.67	0.85	34	empty
5	245	0.62	0.81	37	empty

Interfaces

1 interface between chains.

A–B · 2700 Å² buried · 52 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 54 modified (engineered).

Compared structures

3N04 · THE CRYSTAL STRUCTURE OF THE alpha-Glucosidase (FAMILY 31) FROM RUMINOCOCCUS OBEUM ATCC… · 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 A5ZY13
Elsewhere: RCSB PDB 3N04 · PDBe 3N04 · UniProt A5ZY13

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