Research workbench
Complex of ALF4-activated gi-alpha-1 with RGS4
Analyse Complex of ALF4-activated gi-alpha-1 with RGS4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1AGR
- Type
- protein
- Length
- 938 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P10824, P49799
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 350 | — | P10824 |
| D | — | protein | 344 | — | P10824 |
| E | — | protein | 128 | — | P49799 |
| H | — | protein | 116 | — | P49799 |
Compared structures
- 1AGR · Complex of ALF4-activated gi-alpha-1 with RGS4 · the same entry in another collection · chain H against H, TM-score 1.00
- P49799 · AlphaFold monomer V2.0 prediction for regulator of G-protein signaling 4 (P49799) · a predicted model of the same protein · chain E against A, TM-score 0.99
- P10824 · AlphaFold monomer V2.0 prediction for guanine nucleotide-binding protein G(I) subunit… · a predicted model of the same protein · chain D against A, TM-score 0.94
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 P10824
- Every structure of UniProt P49799
- Elsewhere: RCSB PDB 1AGR · PDBe 1AGR · UniProt P10824 · UniProt P49799
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