› 1hur

X-ray diffraction
2Å resolution

HUMAN ADP-RIBOSYLATION FACTOR 1 COMPLEXED WITH GDP, FULL LENGTH NON-MYRISTOYLATED

Released:
DOI: 10.2210/pdb1hur/pdb
PDB entry 1hur coloured by chain, front view.
PDB entry 1hur coloured by chain, side view.
PDB entry 1hur coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of the human ADP-ribosylation factor 1 complexed with GDP.
Amor JC, Harrison DH, Kahn RA, Ringe D
Nature 372 704-8 (1994)
PMID: 7990966

Function and Biology Details

Reaction catalysed: 
GTP + H(2)O = GDP + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160798 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ADP-ribosylation factor 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 180 amino acids
Theoretical weight: 20.59 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P84077 (Residues: 2-181; Coverage: 99%)
Gene name: ARF1
Sequence domains: ADP-ribosylation factor family
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

2 bound ligands:
Ligand MG 2 x MG
Ligand GDP 2 x GDP
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 121.01Å b: 45.92Å c: 91.78Å
α: 90° β: 133.51° γ: 90°
R-values:
R R work R free
0.213 0.213 0.309
Expression system: Escherichia coli

Quick links

Citations

44 review citations

Small GTP-binding proteins.
Takai et al. (2001)
43 more

27 mentions without citation

The Ras protein superfamily: evolutionary tree and role of conserved amino acids.
Rojas et al. (2012)
26 more