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Structure of beta-hexosaminidase from vibrio cholerae

Analyse Structure of beta-hexosaminidase from vibrio cholerae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1TR9
Type: protein
Length: 330 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-hexosaminidase
EC: 3.2.1.52
UniProt: Q9KU37
Pockets: 2 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-hexosaminidase (EC 3.2.1.52)	protein	330	43% helix, 13% strand	Q9KU37

Pockets

2 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	322	0.60	0.77	29	empty
2	77	0.56	0.87	20	empty

Modifications

Observed in the structure: 12 modified (engineered).

Compared structures

1TR9 · Structure of beta-hexosaminidase from Vibrio cholerae · the same entry in another collection · chain A against A, TM-score 1.00
Q9KU37 · AlphaFold monomer V2.0 prediction for beta-hexosaminidase (Q9KU37) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 Q9KU37
Elsewhere: RCSB PDB 1TR9 · PDBe 1TR9 · UniProt Q9KU37

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