Research workbench
Structural basis for the activation of plc-gamma isozymes by phosphorylation and cancer-associated mutations
Analyse Structural basis for the activation of plc-gamma isozymes by phosphorylation… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6PBC
- Type
- protein
- Length
- 1,070 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase GAMMA,1-phosphatidylinositol…
- EC
- 3.1.4.11
- UniProt
- G3V845, P10686
- Ligands
- CA, NA
- Pockets
- 11 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase GAMMA,1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 (EC 3.1.4.11) | protein | 1070 | 27% helix, 30% strand | G3V845, P10686 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 954 | 0.76 | 0.79 | 106 | empty |
| 2 | 546 | 0.70 | 0.80 | 66 | empty |
| 3 | 226 | 0.60 | 0.80 | 27 | empty |
| 4 | 144 | 0.58 | 0.83 | 26 | empty |
| 5 | 183 | 0.57 | 0.80 | 27 | empty |
Compared structures
- 6PBC · Structural basis for the activation of PLC-gamma isozymes by phosphorylation and… · the same entry in another collection · chain A against A, TM-score 1.00
- P10686 · AlphaFold monomer V2.0 prediction for 1-phosphatidylinositol 4,5-bisphosphate… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 G3V845
- Every structure of UniProt P10686
- Elsewhere: RCSB PDB 6PBC · PDBe 6PBC · UniProt G3V845 · UniProt P10686
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