› 4jif

X-ray diffraction
1.7Å resolution

Co-crystal structure of ICAP1 PTB domain in complex with a KRIT1 peptide

Released:
DOI: 10.2210/pdb4jif/pdb
PDB entry 4jif coloured by chain, front view.
PDB entry 4jif coloured by chain, side view.
PDB entry 4jif coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Cocrystal structure of the ICAP1 PTB domain in complex with a KRIT1 peptide.
Liu W, Boggon TJ
Acta Crystallogr Sect F Struct Biol Cryst Commun 69 494-8 (2013)
PMID: 23695561

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-126333 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Integrin beta-1-binding protein 1 Chain: A
Molecule details ›
Chain: A
Length: 154 amino acids
Theoretical weight: 16.91 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O14713 (Residues: 49-200; Coverage: 76%)
Gene names: ICAP1, ITGB1BP1
Sequence domains: Beta-1 integrin binding protein
Krev interaction trapped protein 1 Chain: B
Molecule details ›
Chain: B
Length: 34 amino acids
Theoretical weight: 3.73 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O00522 (Residues: 170-198; Coverage: 4%)
Gene names: CCM1, KRIT1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P6522
Unit cell:
a: 81.017Å b: 81.017Å c: 89.583Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.197 0.196 0.226
Expression system: Escherichia coli

Quick links

Citations

1 review citation

CCM1 and the second life of proteins in adhesion complexes.
van den Berg et al. (2014)
3 other articles

3 mentions without citation

Structural basis for the disruption of the cerebral cavernous malformations 2 (CCM2) interaction with Krev interaction trapped 1 (KRIT1) by disease-associated mutations.
Fisher et al. (2015)
2 more