MolNFT v1 · #102137 · protein

N-acetylhexosamine 1-phosphate KINASE_ATCC15697 in complex with glcnac

4OCU: “N-acetylhexosamine 1-phosphate KINASE_ATCC15697 in complex with glcnac”. X-ray diffraction, 2 ligands (NDG, SO4), 4 pockets (best druggability 0.78). MolNFT v1 #102137 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4OCU
Type: protein
Length: 356 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: B7GN78
Ligands: NDG, SO4
Pockets: 4 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	N-acetylhexosamine 1-phosphate kinase (EC 2.7.1.162)	protein	356	49% helix, 15% strand	B7GN78

Ligands and binding sites

NDG · 2-acetamido-2-deoxy-alpha-D-glucopyranose · sugar · chains A
SO4 · Sulfate ion · ion · 5 copies · chains A

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

Pockets

4 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	501	0.78	0.85	56	NDG, SO4
2	102	0.48	0.80	18	empty
3	119	0.44	0.77	17	empty
4	67	0.38	0.79	17	empty

Compared structures

4OCU · N-acetylhexosamine 1-phosphate kinase_ATCC15697 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 B7GN78
Elsewhere: RCSB PDB 4OCU · PDBe 4OCU · UniProt B7GN78

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