› 2qa7

X-ray diffraction
2.8Å resolution

Crystal structure of Huntingtin-interacting protein 1 (HIP1) coiled-coil domain with a basic surface suitable for HIP-protein interactor (HIPPI)

Released:
DOI: 10.2210/pdb2qa7/pdb
PDB entry 2qa7 coloured by chain, front view.
PDB entry 2qa7 coloured by chain, side view.
PDB entry 2qa7 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure at 2.8 A of Huntingtin-interacting protein 1 (HIP1) coiled-coil domain reveals a charged surface suitable for HIP1 protein interactor (HIPPI).
Niu Q, Ybe JA
J. Mol. Biol. 375 1197-205 (2008)
PMID: 18155047

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-126227 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Huntingtin-interacting protein 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 114 amino acids
Theoretical weight: 13.48 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O00291 (Residues: 370-481; Coverage: 11%)
Gene name: HIP1
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: P43
Unit cell:
a: 72.9Å b: 72.9Å c: 106.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.32 0.265 0.324
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Molecular structure, function, and dynamics of clathrin-mediated membrane traffic.
Kirchhausen et al. (2014)
1 more

5 mentions without citation

Unconventional functions for clathrin, ESCRTs, and other endocytic regulators in the cytoskeleton, cell cycle, nucleus, and beyond: links to human disease.
Brodsky et al. (2014)
4 more