› 2d1x

X-ray diffraction
1.9Å resolution

The crystal structure of the cortactin-SH3 domain and AMAP1-peptide complex

Released:
DOI: 10.2210/pdb2d1x/pdb
PDB entry 2d1x coloured by chain, front view.
PDB entry 2d1x coloured by chain, side view.
PDB entry 2d1x coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Targeting AMAP1 and cortactin binding bearing an atypical src homology 3/proline interface for prevention of breast cancer invasion and metastasis.
Hashimoto S, Hirose M, Hashimoto A, Morishige M, Yamada A, Hosaka H, Akagi K, Ogawa E, Oneyama C, Agatsuma T, Okada M, Kobayashi H, Wada H, Nakano H, Ikegami T, Nakagawa A, Sabe H
Proc Natl Acad Sci U S A 103 7036-41 (2006)
PMID: 16636290

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171980 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Src substrate cortactin Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 66 amino acids
Theoretical weight: 7.35 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q14247 (Residues: 490-550; Coverage: 11%)
Gene names: CTTN, EMS1
Sequence domains: Variant SH3 domain
Structure domains: SH3 Domains
Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 Chains: P, Q
Molecule details ›
Chains: P, Q
Length: 15 amino acids
Theoretical weight: 1.69 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q9ULH1 (Residues: 823-837; Coverage: 1%)
Gene names: ASAP1, DDEF1, KIAA1249, PAG2

Ligands and Environments

1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: C2221
Unit cell:
a: 71.45Å b: 132.14Å c: 61.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.216 0.226
Expression systems:
  • Escherichia coli BL21
  • Not provided

Quick links

Citations

20 review citations

Ras superfamily GEFs and GAPs: validated and tractable targets for cancer therapy?
Vigil et al. (2010)
19 more

4 mentions without citation

Characterization of domain-peptide interaction interface: prediction of SH3 domain-mediated protein-protein interaction network in yeast by generic structure-based models.
Hou et al. (2012)
3 more