› 1srq

X-ray diffraction
2.9Å resolution

Crystal Structure of the Rap1GAP catalytic domain

Released:
DOI: 10.2210/pdb1srq/pdb
PDB entry 1srq coloured by chain, front view.
PDB entry 1srq coloured by chain, side view.
PDB entry 1srq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The GTPase-activating protein Rap1GAP uses a catalytic asparagine.
Daumke O, Weyand M, Chakrabarti PP, Vetter IR, Wittinghofer A
Nature 429 197-201 (2004)
PMID: 15141215

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155647 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Rap1 GTPase-activating protein 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 341 amino acids
Theoretical weight: 38.96 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P47736 (Residues: 75-415; Coverage: 51%)
Gene names: KIAA0474, RAP1GA1, RAP1GAP
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand SO4 2 x SO4
Ligand MPD 2 x MPD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P21212
Unit cell:
a: 170.7Å b: 224.5Å c: 48.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.234 0.232 0.276
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

21 review citations

GEFs and GAPs: critical elements in the control of small G proteins.
Bos et al. (2007)
20 more

7 mentions without citation

Control of TSC2-Rheb signaling axis by arginine regulates mTORC1 activity.
Carroll et al. (2016)
6 more