Research workbench
Crystal structure of phosphatidyl inositol 4-kinase II alpha in complex with ATP
Analyse Crystal structure of phosphatidyl inositol 4-kinase II alpha in complex with ATP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4PLA
- Type
- protein
- Length
- 483 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chimera protein of phosphatidylinositol 4-kinase type 2- alpha and lysozyme
- EC
- 2.7.1.67, 3.2.1.17
- UniProt
- Q9BTU6, D9IEF7
- Ligands
- ATP
- Pockets
- 4 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chimera protein of phosphatidylinositol 4-kinase type 2- alpha and lysozyme (EC 2.7.1.67, 3.2.1.17) | protein | 483 | 51% helix, 11% strand | Q9BTU6, D9IEF7 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 2 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 642 | 0.69 | 0.77 | 81 | ATP |
| 2 | 231 | 0.53 | 0.76 | 28 | empty |
| 3 | 104 | 0.49 | 0.80 | 16 | ATP |
| 4 | 163 | 0.43 | 0.74 | 26 | empty |
Compared structures
- 4PLA · Crystal structure of phosphatidyl inositol 4-kinase II alpha in complex with ATP · the same entry in another collection · chain A against A, TM-score 1.00
- Q9BTU6 · AlphaFold monomer V2.0 prediction for phosphatidylinositol 4-kinase type 2-alpha (Q9BTU6) · a predicted model of the same protein · chain A against A, TM-score 0.64
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 Q9BTU6
- Every structure of UniProt D9IEF7
- Elsewhere: RCSB PDB 4PLA · PDBe 4PLA · UniProt Q9BTU6 · UniProt D9IEF7
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