› 1wer

X-ray diffraction
1.6Å resolution

RAS-GTPASE-ACTIVATING DOMAIN OF HUMAN P120GAP

Released:
DOI: 10.2210/pdb1wer/pdb
PDB entry 1wer coloured by chain, front view.
PDB entry 1wer coloured by chain, side view.
PDB entry 1wer coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the GTPase-activating domain of human p120GAP and implications for the interaction with Ras.
Scheffzek K, Lautwein A, Kabsch W, Ahmadian MR, Wittinghofer A
Nature 384 591-6 (1996)
PMID: 8955277

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149093 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ras GTPase-activating protein 1 Chain: A
Molecule details ›
Chain: A
Length: 334 amino acids
Theoretical weight: 38.22 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P20936 (Residues: 714-1047; Coverage: 32%)
Gene names: GAP, RASA, RASA1
Sequence domains: GTPase-activator protein for Ras-like GTPase
Structure domains: GTPase Activation - p120gap; domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID2
Spacegroup: P212121
Unit cell:
a: 42.2Å b: 55.6Å c: 142.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.221 0.221 0.271
Expression system: Escherichia coli

Quick links

Citations

23 review citations

G protein mechanisms: insights from structural analysis.
Sprang SR. (1997)
22 more

18 mentions without citation

Overview of protein structural and functional folds.
Sun et al. (2004)
17 more