Research workbench
Structure of the phospholipase C gamma 1 TSH2 domain in complex with a phosphorylated kshv PK15 peptide
Analyse Structure of the phospholipase C gamma 1 TSH2 domain in complex with a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7NXE
- Type
- protein
- Length
- 228 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Isoform 2 of 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1; Protein…
- EC
- 3.1.4.11
- UniProt
- P19174, Q9QR69
- Pockets
- 2 · best druggability 0.36
Structure
x-ray diffraction · 3 distinct chains · 24% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Isoform 2 of 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 (EC 3.1.4.11) | protein | 219 | 25% helix, 32% strand | P19174 |
| C | Protein K15 | protein | 7 | 0% helix, 0% strand | Q9QR69 |
| D | Protein K15 | protein | 2 | 0% helix, 0% strand | Q9QR69 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 108 | 0.36 | 0.74 | 21 | empty |
| 2 | 58 | 0.30 | 0.75 | 18 | empty |
Interfaces
2 interfaces between chains.
- A–C · 505 Ų buried · 8 hydrogen bonds · protein-protein
- A–D · 345 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
- 7NXE · Structure of the Phospholipase C gamma 1 tSH2 domain in complex with a phosphorylated… · the same entry in another collection · chain A against A, TM-score 1.00
- P19174 · AlphaFold monomer V2.0 prediction for 1-phosphatidylinositol 4,5-bisphosphate… · a predicted model of the same protein · chain A against A, TM-score 0.95
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 P19174
- Every structure of UniProt Q9QR69
- Elsewhere: RCSB PDB 7NXE · PDBe 7NXE · UniProt P19174 · UniProt Q9QR69
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.