MolNFT v1 · #117298 · protein

Crystal structure of phosphatidylinositol-4-phosphate 5-kinase

5E3U · Phosphatidylinositol-4-phosphate 5-kinase, type I, alpha: “Crystal structure of phosphatidylinositol-4-phosphate 5-kinase”. X-ray diffraction, 3 ligands (ANP, MN, SE4), 2 pockets (best druggability 0.65). MolNFT v1 #117298 on…

PDB: 5E3U
Type: protein
Length: 302 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphatidylinositol-4-phosphate 5-kinase, type I, alpha
UniProt: Q503I3
Ligands: ANP, MN, SE4
Pockets: 2 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphatidylinositol-4-phosphate 5-kinase, type I, alpha	protein	302	37% helix, 24% strand	Q503I3

Ligands and binding sites

ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains A
MN · Manganese (II) ion · metal · 2 copies · chains A
SE4 · Selenate ion · ion · 2 copies · 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	465	0.65	0.78	51	ANP, MN
2	217	0.48	0.74	30	empty

Compared structures

5E3U · Crystal structure of phosphatidylinositol-4-phosphate 5-kinase · 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 Q503I3
Elsewhere: RCSB PDB 5E3U · PDBe 5E3U · UniProt Q503I3

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.