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Crystal structure of streptomyces plicatus beta-N-acetylhexosaminidase

Analyse Crystal structure of streptomyces plicatus beta-N-acetylhexosaminidase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1HP4
Type: protein
Length: 499 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-N-acetylhexosaminidase
EC: 3.2.1.52
UniProt: O85361
Ligands: CL, SO4
Pockets: 5 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-N-acetylhexosaminidase (EC 3.2.1.52)	protein	499	34% helix, 17% strand	O85361

Ligands and binding sites

CL · Chloride ion · ion · 4 copies · chains A
SO4 · Sulfate ion · ion · chains A
GOL · Glycerol · additive · 3 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	63	0.54	0.87	16	GOL
2	111	0.42	0.77	18	CL
3	54	0.39	0.81	15	empty
4	111	0.37	0.74	21	GOL
5	89	0.32	0.73	16	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

1HP4 · Crystal structure of streptomyces plicatus beta-N-acetylhexosaminidase · 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 O85361
Elsewhere: RCSB PDB 1HP4 · PDBe 1HP4 · UniProt O85361

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