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N-acetylhexosamine 1-phosphate kinase in complex with glcnac

Analyse N-acetylhexosamine 1-phosphate kinase in complex with glcnac in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4OCJ
Type: protein
Length: 355 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: N-acetylhexosamine 1-phosphate kinase
EC: 2.7.1.162
UniProt: T2I3Q3
Ligands: NDG, NA
Pockets: 5 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	N-acetylhexosamine 1-phosphate kinase (EC 2.7.1.162)	protein	355	49% helix, 14% strand	T2I3Q3

Ligands and binding sites

NDG · 2-acetamido-2-deoxy-alpha-D-glucopyranose · sugar · chains A
NA · Sodium ion · metal · chains A

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

Pockets

5 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	356	0.80	0.90	47	NDG
2	87	0.45	0.80	17	empty
3	94	0.42	0.78	19	empty
4	89	0.41	0.78	16	empty
5	68	0.38	0.79	16	empty

Modifications

Observed in the structure: 10 modified (engineered).

Compared structures

4OCJ · N-acetylhexosamine 1-phosphate kinase in complex with GlcNAc · 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 T2I3Q3
Elsewhere: RCSB PDB 4OCJ · PDBe 4OCJ · UniProt T2I3Q3

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