Research workbench
Crystal structure of zebrafish phosphatidylinositol-4-phosphate 5- kinase alpha isoform D236N with bound ATP/CA2+
Analyse Crystal structure of zebrafish phosphatidylinositol-4-phosphate 5- kinase alpha… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6CN2
- Type
- protein
- Length
- 300 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
- ATP, CA
- Pockets
- 1 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphatidylinositol-4-phosphate 5-kinase, type I, alpha | protein | 300 | 36% helix, 24% strand | Q503I3 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 620 | 0.68 | 0.77 | 64 | ATP |
Compared structures
- 6CN2 · Crystal structure of zebrafish Phosphatidylinositol-4-phosphate 5- kinase alpha isoform… · 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 6CN2 · PDBe 6CN2 · UniProt Q503I3
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