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Crystal structure of endo-beta-N-acetylglucosaminidase H at 1.9 ångströms resolution: active site geometry and substrate recognition

Analyse Crystal structure of endo-beta-N-acetylglucosaminidase H at 1.9 ångströms… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1EDT
Type: protein
Length: 265 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endo-beta-N-acetylglucosaminidase H, endo H
EC: 3.2.1.96
UniProt: P04067
Pockets: 1 · best druggability 0.37

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endo-beta-N-acetylglucosaminidase H, endo H (EC 3.2.1.96)	protein	265	34% helix, 26% strand	P04067

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	55	0.37	0.79	17	empty

Compared structures

1EDT · Crystal structure of endo-beta-N-acetylglucosaminidase H at 1.9 ångströms resolution… · the same entry in another collection · chain A against A, TM-score 1.00
P04067 · AlphaFold monomer V2.0 prediction for endo-beta-N- acetylglucosaminidase H (P04067) · a predicted model of the same protein · 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 P04067
Elsewhere: RCSB PDB 1EDT · PDBe 1EDT · UniProt P04067

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