Research workbench
Structure of the px domain of phosphoinositide 3-kinase-C2ALPHA
Analyse Structure of the px domain of phosphoinositide 3-kinase-C2ALPHA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2IWL
- Type
- protein
- Length
- 121 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphatidylinositol-4-phosphate 3-kinase C2 domain- containing alpha polypeptide
- EC
- 2.7.1.154, 2.7.1.137
- UniProt
- O00443
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Phosphatidylinositol-4-phosphate 3-kinase C2 domain- containing alpha polypeptide (EC 2.7.1.154, 2.7.1.137) | protein | 121 | 37% helix, 21% strand | O00443 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains X
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2IWL · Structure of the PX Domain of Phosphoinositide 3-Kinase-C2alpha · the same entry in another collection · chain X against X, TM-score 1.00
- O00443 · AlphaFold monomer V2.0 prediction for phosphatidylinositol 4-phosphate 3-kinase C2… · a predicted model of the same protein · chain X against A, TM-score 0.96
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 O00443
- Elsewhere: RCSB PDB 2IWL · PDBe 2IWL · UniProt O00443
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