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LMO2764 protein, a putative N-acetylmannosamine kinase, from listeria monocytogenes

Analyse LMO2764 protein, a putative N-acetylmannosamine kinase, from listeria… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4HTL
Type: protein
Length: 291 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-glucoside kinase
EC: 2.7.1.85
UniProt: Q8Y3R9
Pockets: 2 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-glucoside kinase (EC 2.7.1.85)	protein	291	43% helix, 23% strand	Q8Y3R9

Ligands and binding sites

EDO · 1,2-ethanediol · additive · chains A

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

Pockets

2 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	505	0.66	0.78	55	empty
2	72	0.30	0.74	20	empty

Modifications

Observed in the structure: 7 modified (engineered).

Compared structures

4HTL · Lmo2764 protein, a putative N-acetylmannosamine kinase, from Listeria monocytogenes · the same entry in another collection · chain A against A, TM-score 1.00
Q8Y3R9 · AlphaFold monomer V2.0 prediction for beta-glucoside kinase (Q8Y3R9) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q8Y3R9
Elsewhere: RCSB PDB 4HTL · PDBe 4HTL · UniProt Q8Y3R9

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