MolNFT v1 · #11218 · protein
AlphaFold monomer V2.0 prediction for arf-gap domain and fg repeat- containing protein 1 (P52594)
P52594: “AlphaFold monomer V2.0 prediction for arf-gap domain and fg repeat- containing protein 1 (P52594)”. MolNFT v1 #11218 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- P52594
- Type
- protein
- Length
- 562 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5ce0D3c69518629Fa692C944CeBE0a3596343B38
- UniProt
- P52594
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 562 | — | P52594 |
Compared structures
- 2OLM · Arfgap domain of HIV-1 rev binding protein · an experimental structure of the same protein · chain A against A, TM-score 0.23
- 2OLM · ArfGap domain of HIV-1 Rev binding protein · an experimental structure of the same protein · chain A against A, TM-score 0.23
- 2D9L · Solution structure of the ArfGap domain of human RIP · an experimental structure of the same protein · chain A against A, TM-score 0.22
- 2D9L · Solution structure of the arfgap domain of human rip · an experimental structure of the same protein · chain A against A, TM-score 0.22
- 2VX8 · Vamp7 longin domain Hrb peptide complex · an experimental structure of the same protein · chain A against D, TM-score 0.12
- 2VX8 · VAMP7 longin domain hrb peptide complex · an experimental structure of the same protein · chain A against D, TM-score 0.12
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 P52594
- Elsewhere: UniProt P52594 · AlphaFold DB P52594
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