Research workbench
Crystal structure of the C2 domain of class II phosphatidylinositide 3-kinase C2
Analyse Crystal structure of the C2 domain of class II phosphatidylinositide 3-kinase C2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2B3R
- Type
- protein
- Length
- 248 residues
- Chains
- 2
- 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
- UniProt
- Q61194
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Phosphatidylinositol-4-phosphate 3-kinase C2 domain- containing alpha polypeptide (EC 2.7.1.154) | protein | 124 | 6% helix, 50% strand | Q61194 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 6 copies · chains A, B
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.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 260 | 0.57 | 0.78 | 34 | empty |
| 2 | 67 | 0.41 | 0.80 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 434 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 2B3R · Crystal structure of the C2 domain of class II phosphatidylinositide 3-kinase C2 · the same entry in another collection · chain A against A, TM-score 1.00
- Q61194 · AlphaFold monomer V2.0 prediction for phosphatidylinositol 4-phosphate 3-kinase C2… · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q61194
- Elsewhere: RCSB PDB 2B3R · PDBe 2B3R · UniProt Q61194
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