› 3i6x

X-ray diffraction
2.5Å resolution

Crystal structure of the calponin homology domain of IQGAP1

Released:
DOI: 10.2210/pdb3i6x/pdb
PDB entry 3i6x coloured by chain, front view.
PDB entry 3i6x coloured by chain, side view.
PDB entry 3i6x coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The IQGAP1 N-Terminus Forms Dimers, and the Dimer Interface Is Required for Binding F-Actin and Calcium-Bound Calmodulin.
Liu J, Kurella VB, LeCour L, Vanagunas T, Worthylake DK
Biochemistry 55 6433-6444 (2016)
PMID: 27798963

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155564 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ras GTPase-activating-like protein IQGAP1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 193 amino acids
Theoretical weight: 22.39 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P46940 (Residues: 1-191; Coverage: 12%)
Gene names: IQGAP1, KIAA0051
Sequence domains: Calponin homology (CH) domain
Structure domains: Calponin-like domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 31-ID
Spacegroup: P1
Unit cell:
a: 57.432Å b: 66.421Å c: 83.014Å
α: 99.55° β: 104.07° γ: 108.69°
R-values:
R R work R free
0.234 0.234 0.263
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Pleiotropic Roles of Calmodulin in the Regulation of KRas and Rac1 GTPases: Functional Diversity in Health and Disease.
Tebar et al. (2020)
1 more

4 mentions without citation

The IQGAP1 N-Terminus Forms Dimers, and the Dimer Interface Is Required for Binding F-Actin and Calcium-Bound Calmodulin.
Liu et al. (2016)
3 more