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Crystal structure of the endo-beta-N-acetylglucosaminidase from thermotoga maritima

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

PDB: 4QDN
Type: protein
Length: 118 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Flagellar protein flgj [peptidoglycan hydrolase]
EC: 3.2.1.-
UniProt: Q9WZA1
Ligands: PO4
Pockets: 1 · best druggability 0.35

Structure

x-ray diffraction · 1 distinct chain · 61% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Flagellar protein flgj [peptidoglycan hydrolase] (EC 3.2.1.-)	protein	118	61% helix, 2% strand	Q9WZA1

Ligands and binding sites

PO4 · Phosphate ion · ion · chains A
MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains A

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

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	73	0.35	0.76	15	MPD

Compared structures

4QDN · Crystal Structure of the endo-beta-N-acetylglucosaminidase from Thermotoga maritima · 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 Q9WZA1
Elsewhere: RCSB PDB 4QDN · PDBe 4QDN · UniProt Q9WZA1

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