› 1n5z

X-ray diffraction
2.7Å resolution

Complex structure of Pex13p SH3 domain with a peptide of Pex14p

Released:
DOI: 10.2210/pdb1n5z/pdb
PDB entry 1n5z coloured by chain, front view.
PDB entry 1n5z coloured by chain, side view.
PDB entry 1n5z coloured by chain, top view.
Source organisms:
Primary publication:
Topography for independent binding of alpha-helical and PPII-helical ligands to a peroxisomal SH3 domain.
Douangamath A, Filipp FV, Klein AT, Barnett P, Zou P, Voorn-Brouwer T, Vega MC, Mayans OM, Sattler M, Distel B, Wilmanns M
Mol Cell 10 1007-17 (2002)
PMID: 12453410

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-156716 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Peroxisomal membrane protein PEX13 Chains: A, B
Molecule details ›
Chains: A, B
Length: 92 amino acids
Theoretical weight: 10.78 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P80667 (Residues: 299-386; Coverage: 23%)
Gene names: L9470.1, PAS20, PEX13, YLR191W
Sequence domains: SH3 domain
Structure domains: SH3 Domains
Peroxisomal membrane protein PEX14 Chains: P, Q
Molecule details ›
Chains: P, Q
Length: 14 amino acids
Theoretical weight: 1.7 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Not provided
UniProt:
  • Canonical: P53112 (Residues: 83-96; Coverage: 4%)
Gene names: G1870, PEX14, YGL153W

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X31
Spacegroup: P212121
Unit cell:
a: 50.35Å b: 63.204Å c: 66.935Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.246 0.244 0.273
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

18 review citations

Specificity and versatility of SH3 and other proline-recognition domains: structural basis and implications for cellular signal transduction.
Li SS. (2005)
17 more

10 mentions without citation

Topography for independent binding of alpha-helical and PPII-helical ligands to a peroxisomal SH3 domain.
Douangamath et al. (2002)
9 more