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Crystal structure of Listeria innocua D-Tagatose-6-Phosphate Kinase bound with substrate

Analyse Crystal structure of Listeria innocua D-Tagatose-6-Phosphate Kinase bound with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3JUL
Type: protein
Length: 298 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.4
Source: Listeria innocua
Molecule: Lin2199 protein
EC: 2.7.1.144
UniProt: Q929S5
Ligands: TA6, MG
Pockets: 1 · best druggability 0.70

Structure

x-ray diffraction · resolution 2.4 · 1 distinct chain · 38% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lin2199 protein (EC 2.7.1.144)	protein	298	38% helix, 26% strand	Q929S5

Ligands and binding sites

TA6 · 6-O-phosphono-beta-D-tagatofuranose · sugar · chains A
MG · Magnesium ion · metal · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	596	0.70	0.79	70	MG, TA6

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

3JUL · Crystal structure of listeria innocua D-tagatose-6-phosphate kinase bound with substrate · 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 Q929S5
Elsewhere: RCSB PDB 3JUL · PDBe 3JUL · UniProt Q929S5

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