X-ray diffraction
1.58Å resolution

Crystal structure of the 2nd SH3 domain from human CD2AP (CMS) in complex with a proline-rich peptide (aa 76-91) from human ARAP1

Source organism: Homo sapiens
Entry authors: Rouka E, Krojer T, von Delft F, Knapp S, Kirsch KH, Arrowsmith CH, Edwards AM, Bountra C, Feller SM, Simister PC

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
CD2-associated protein Chain: A
Molecule details ›
Chain: A
Length: 65 amino acids
Theoretical weight: 7.44 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: Q9Y5K6 (Residues: 109-168; Coverage: 9%)
Gene name: CD2AP
Sequence domains: Variant SH3 domain
Structure domains: SH3 Domains
Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 1 Chain: B
Molecule details ›
Chain: B
Length: 16 amino acids
Theoretical weight: 1.98 KDa
Source organism: Homo sapiens
Expression system: Not provided
  • Canonical: Q96P48 (Residues: 76-91; Coverage: 1%)
Gene names: ARAP1, CENTD2, KIAA0782

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P43
Unit cell:
a: 44.59Å b: 44.59Å c: 32.94Å
α: 90° β: 90° γ: 90°
R R work R free
0.162 0.16 0.2
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided