MolNFT v1 · #81702 · protein
Studies of a constitutively active G-alpha subunit provide insights into the mechanism of G protein activation.
3V00: “Studies of a constitutively active G-alpha subunit provide insights into the mechanism of G protein…”. X-ray diffraction. MolNFT v1 #81702 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3V00
- Type
- protein
- Length
- 1,046 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P04695, P10824
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | — | protein | 353 | — | P04695, P10824 |
| B | — | protein | 342 | — | P04695, P10824 |
| A | — | protein | 351 | — | P04695, P10824 |
Compared structures
- 3V00 · Studies of a constitutively active G-alpha subunit provide insights into the mechanism of… · the same entry in another collection · chain C against C, TM-score 1.00
- P10824 · AlphaFold monomer V2.0 prediction for guanine nucleotide-binding protein G(I) subunit… · a predicted model of the same protein · chain B against A, TM-score 0.93
- P04695 · AlphaFold monomer V2.0 prediction for guanine nucleotide-binding protein G(T) subunit… · a predicted model of the same protein · chain B against A, TM-score 0.91
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 P04695
- Every structure of UniProt P10824
- Elsewhere: RCSB PDB 3V00 · PDBe 3V00 · UniProt P04695 · UniProt P10824
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