Research workbench
Tertiary and quaternary structural changes in GIA1 induced by GTP hydrolysis
Analyse Tertiary and quaternary structural changes in GIA1 induced by GTP hydrolysis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GDD
- Type
- protein
- Length
- 324 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P10824
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 324 | — | P10824 |
Compared structures
- 1GDD · Tertiary and quaternary structural changes in GIA1 induced by GTP hydrolysis · the same entry in another collection · chain A against A, 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 A 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 P10824
- Elsewhere: RCSB PDB 1GDD · PDBe 1GDD · UniProt P10824
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