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Non-myristoylated rat ADP-ribosylation factor-1 complexed with GDP, dimeric crystal form

Analyse Non-myristoylated rat ADP-ribosylation factor-1 complexed with GDP, dimeric… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1RRG
Type
protein
Length
354 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Rat ADP-ribosylation factor-1
UniProt
P84079
Ligands
GDP, MG
Pockets
1 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BRat ADP-ribosylation factor-1protein17734% helix, 27% strandP84079

Ligands and binding sites

  • GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains A, B
  • MG · Magnesium ion · metal · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14320.630.7756MG, GDP

Interfaces

1 interface between chains.

  • A–B · 586 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 1RRG · Non-myristoylated rat ADP-ribosylation factor-1 complexed with GDP, dimeric 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 0.81

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