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Crystal structure of human phosphatidylinositol-5-phosphate 4-kinase type-2 alpha

Analyse Crystal structure of human phosphatidylinositol-5-phosphate 4-kinase type-2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2YBX
Type
protein
Length
634 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Phosphatidylinositol-5-phosphate 4-kinase type-2 alpha
EC
2.7.1.149
UniProt
P48426
Ligands
PO4
Pockets
7 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APhosphatidylinositol-5-phosphate 4-kinase type-2 alpha (EC 2.7.1.149)protein32236% helix, 23% strandP48426
BPhosphatidylinositol-5-phosphate 4-kinase type-2 alpha (EC 2.7.1.149)protein31235% helix, 24% strandP48426

Ligands and binding sites

  • PO4 · Phosphate ion · ion · chains A

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

Pockets

7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1990.750.9630empty
24810.680.7957empty
33620.670.8042empty
41190.440.7721empty
51010.410.7720empty

Interfaces

1 interface between chains.

  • A–B · 1485 Ų buried · 29 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (phosphorylation).

Compared structures

  • 2YBX · Crystal Structure of Human Phosphatidylinositol-5-phosphate 4-kinase type-2 alpha · the same entry in another collection · chain A against A, TM-score 1.00
  • P48426 · AlphaFold monomer V2.0 prediction for phosphatidylinositol 5-phosphate 4-kinase type-2… · a predicted model of the same protein · chain A against A, TM-score 0.99

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