Research workbench
Non-myristoylated rat ADP-ribosylation factor-1 complexed with GDP, monomeric crystal form
Analyse Non-myristoylated rat ADP-ribosylation factor-1 complexed with GDP, monomeric… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1RRF
- Type
- protein
- Length
- 175 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3
- Source
- Rattus norvegicus
- Molecule
- Rat ADP-ribosylation factor-1
- UniProt
- P84079
- Ligands
- GDP, MG
Structure
x-ray diffraction · resolution 3 · 1 distinct chain · 26% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Rat ADP-ribosylation factor-1 | protein | 175 | 26% helix, 28% strand | P84079 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1RRF · Non-myristoylated rat ADP-ribosylation factor-1 complexed with GDP, monomeric crystal form · the same entry in another collection · chain A against A, TM-score 1.00
- P84079 · AlphaFold monomer V2.0 prediction for ADP-ribosylation factor 1 (P84079) · a predicted model of the same protein · chain A against A, TM-score 0.80
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 P84079
- Elsewhere: RCSB PDB 1RRF · PDBe 1RRF · UniProt P84079
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.