3w6r

X-ray diffraction
1.9Å resolution

Crystal structure of the GAP domain of human MgcRacGAP

Released:
Source organism: Homo sapiens
Primary publication:
Crystal structure of GTPase-activating domain from human MgcRacGAP.
Biochem Biophys Res Commun 435 367-72 (2013)
PMID: 23665020

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-190478 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Rac GTPase-activating protein 1 Chain: A
Molecule details ›
Chain: A
Length: 202 amino acids
Theoretical weight: 22.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9H0H5 (Residues: 348-546; Coverage: 32%)
Gene names: KIAA1478, MGCRACGAP, RACGAP1
Sequence domains: RhoGAP domain
Structure domains: Rho GTPase activation protein

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 41.466Å b: 63.159Å c: 74.078Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.223 0.222 0.259
Expression system: Escherichia coli