MolNFT v1 · #187680 · protein
Reprocessed and refined structure of phospholipase C-beta and gq signaling complex
7SQ2: “Reprocessed and refined structure of phospholipase C-beta and gq signaling complex”. X-ray diffraction, 4 ligands (ALF, GDP, MG). MolNFT v1 #187680 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7SQ2
- Type
- protein
- Length
- 1,072 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P21279, Q01970
- Ligands
- ALF, GDP, MG, CA
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 317 | — | P21279 |
| B | — | protein | 755 | — | Q01970 |
Ligands and binding sites
- ALF · Tetrafluoroaluminate ion · ligand · chains A
- GDP · Guanosine-5'-diphosphate · ligand · chains A
- MG · Magnesium ion · metal · 2 copies · chains A, B
- CA · Calcium ion · metal · chains B
- ACT · Acetate ion · additive · 7 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7SQ2 · Reprocessed and refined structure of Phospholipase C-beta and Gq signaling complex · the same entry in another collection · chain A against A, TM-score 1.00
- Q01970 · AlphaFold monomer V2.0 prediction for 1-phosphatidylinositol 4,5-bisphosphate… · a predicted model of the same protein · chain B against A, TM-score 0.99
- P21279 · AlphaFold monomer V2.0 prediction for guanine nucleotide-binding protein G(Q) subunit… · 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 P21279
- Every structure of UniProt Q01970
- Elsewhere: RCSB PDB 7SQ2 · PDBe 7SQ2 · UniProt P21279 · UniProt Q01970
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