› 5l0o

X-ray diffraction
2.36Å resolution

IQGAP1 calponin homology domain fragment (CHDF) mutant K161C under oxidizing conditions

Released:
DOI: 10.2210/pdb5l0o/pdb
PDB entry 5l0o coloured by chain, front view.
PDB entry 5l0o coloured by chain, side view.
PDB entry 5l0o 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: 22.36 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: BRUKER AXS MICROSTAR
Spacegroup: P1
Unit cell:
a: 53.752Å b: 72.464Å c: 73.272Å
α: 77.15° β: 72.07° γ: 86.8°
R-values:
R R work R free
0.262 0.262 0.286
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

1 mention 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)