MolNFT v1 · #160125 · protein
Structural basis for the activation of plc-gamma isozymes by phosphorylation and cancer-associated mutations
6PBC: “Structural basis for the activation of plc-gamma isozymes by phosphorylation and cancer-associated mutations”. X-ray diffraction, 2 ligands (CA, NA). MolNFT v1 #160125 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6PBC
- Type
- protein
- Length
- 1,070 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- G3V845, P10686
- Ligands
- CA, NA
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 1070 | — | G3V845, P10686 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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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