Research workbench
Phosphatidylinositol 3-kinase, P85-alpha subunit: C-terminal SH2 domain complexed with a TYR751 phosphopeptide from the PDGF receptor, NMR, minimized mean structure
Analyse Phosphatidylinositol 3-kinase, P85-alpha subunit: C-terminal SH2 domain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1PIC
- Type
- protein
- Length
- 117 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphatidylinositol 3-kinase; Beta-platelet-derived growth factor receptor
- EC
- 2.7.1.137
- UniProt
- P27986
- Ligands
- ACE
- Pockets
- 1 · best druggability 0.38
Structure
solution nmr · 2 distinct chains · 15% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphatidylinositol 3-kinase (EC 2.7.1.137) | protein | 112 | 16% helix, 20% strand | P27986 |
| B | Beta-platelet-derived growth factor receptor | protein | 5 | 0% helix, 20% strand | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 84 | 0.38 | 0.77 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 585 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent, 1 modified (covalent ligand, phosphorylation).
Compared structures
- 1PIC · Phosphatidylinositol 3-kinase, P85-alpha subunit: C-terminal SH2 domain complexed with a… · the same entry in another collection · chain A against A, TM-score 1.00
- P27986 · AlphaFold monomer V2.0 prediction for phosphatidylinositol 3-kinase regulatory subunit… · a predicted model of the same protein · chain A against A, TM-score 0.85
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 P27986
- Elsewhere: RCSB PDB 1PIC · PDBe 1PIC · UniProt P27986
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.