Research workbench

Crystal structure of GH20 exo beta-N-acetylglucosaminidase from vibrio harveyi

Analyse Crystal structure of GH20 exo beta-N-acetylglucosaminidase from vibrio harveyi in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6EZR
Type: protein
Length: 1,278 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-N-acetylglucosaminidase NAG2
EC: 3.2.1.52
UniProt: D9ISE0
Pockets: 16 · best druggability 0.89

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Beta-N-acetylglucosaminidase NAG2 (EC 3.2.1.52)	protein	639	29% helix, 26% strand	D9ISE0

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1009	0.89	0.90	135	empty
2	612	0.76	0.83	74	empty
3	171	0.58	0.82	37	empty
4	255	0.54	0.76	41	empty
5	159	0.51	0.79	21	empty

Interfaces

1 interface between chains.

A–B · 2180 Å² buried · 25 hydrogen bonds · protein-protein

Compared structures

6EZR · Crystal structure of GH20 Exo beta-N-Acetylglucosaminidase from Vibrio harveyi · 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 D9ISE0
Elsewhere: RCSB PDB 6EZR · PDBe 6EZR · UniProt D9ISE0

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.