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Crystal structure of lactococcus lactis subsp. cremoris GH31 alpha-1, 3-glucosidase, P6322 space group

Analyse Crystal structure of lactococcus lactis subsp. cremoris GH31 alpha-1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7WJA
Type: protein
Length: 729 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-xylosidase
EC: 3.2.1.-
UniProt: A2RM80
Pockets: 10 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-xylosidase (EC 3.2.1.-)	protein	729	29% helix, 24% strand	A2RM80

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 7 copies · chains A

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

Pockets

10 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	330	0.67	0.81	39	EDO
2	405	0.62	0.77	47	EDO
3	82	0.53	0.85	15	empty
4	226	0.52	0.76	29	EDO
5	78	0.40	0.79	21	empty

Compared structures

7WJA · Crystal structure of Lactococcus lactis subsp. cremoris GH31 alpha-1,3-glucosidase, P6322… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt A2RM80
Elsewhere: RCSB PDB 7WJA · PDBe 7WJA · UniProt A2RM80

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