MolNFT v1 · #135072 · protein
Phospholipase C gamma-1 C-terminal SH2 domain
5TNW · 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase…: “Phospholipase C gamma-1 C-terminal SH2 domain”. X-ray diffraction, 1 pocket (best druggability 0.53). MolNFT v1 #135072 on GenesisL1: 3D structure, binding sites and…
- PDB
- 5TNW
- Type
- protein
- Length
- 200 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
- EC
- 3.1.4.11
- UniProt
- P08487
- Pockets
- 1 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 21% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 (EC 3.1.4.11) | protein | 100 | 21% helix, 37% strand | P08487 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 272 | 0.53 | 0.75 | 38 | empty |
Interfaces
1 interface between chains.
- A–B · 550 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
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 P08487
- Elsewhere: RCSB PDB 5TNW · PDBe 5TNW · UniProt P08487
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