MolNFT v1 · #73186 · protein

The crystal structure of the W169Y mutant of alpha-glucosidase (family 31) from ruminococcus obeum atcc 29174

3NUK: “The crystal structure of the W169Y mutant of alpha-glucosidase (family 31) from ruminococcus obeum atcc 29174”. X-ray diffraction, 13 pockets (best druggability 0.88). MolNFT v1 #73186 on GenesisL1: 3D structure, binding sites and…

PDB: 3NUK
Type: protein
Length: 1,314 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-glucosidase
UniProt: A5ZY13
Pockets: 13 · best druggability 0.88

Structure

x-ray diffraction · 2 distinct chains · 28% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-glucosidase	protein	664	28% helix, 26% strand	A5ZY13
B	Alpha-glucosidase	protein	650	28% helix, 26% strand	A5ZY13

Ligands and binding sites

GOL · Glycerol · additive · chains A

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

Pockets

13 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1012	0.88	0.89	97	empty
2	228	0.65	0.84	31	empty
3	467	0.63	0.76	62	GOL
4	220	0.63	0.83	30	empty
5	121	0.57	0.84	16	empty

Interfaces

1 interface between chains.

A–B · 2547 Å² buried · 42 hydrogen bonds · protein-protein

Compared structures

3NUK · THE CRYSTAL STRUCTURE OF THE W169Y mutant of ALPHA-GLUCOSIDASE (FAMILY 31) from… · 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 3NUK · PDBe 3NUK · UniProt A5ZY13

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