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 v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Rat ADP-ribosylation factor-1
- UniProt
- P84079
- Ligands
- GDP, MG
Structure
x-ray diffraction · 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
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