› 1nte

X-ray diffraction
1.24Å resolution

CRYSTAL STRUCTURE ANALYSIS OF THE SECOND PDZ DOMAIN OF SYNTENIN

Released:
DOI: 10.2210/pdb1nte/pdb
PDB entry 1nte coloured by chain, front view.
PDB entry 1nte coloured by chain, side view.
PDB entry 1nte coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Molecular roots of degenerate specificity in syntenin's PDZ2 domain: reassessment of the PDZ recognition paradigm.
Kang BS, Cooper DR, Devedjiev Y, Derewenda U, Derewenda ZS
Structure 11 845-53 (2003)
PMID: 12842047

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-126342 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Syntenin-1 Chain: A
Molecule details ›
Chain: A
Length: 82 amino acids
Theoretical weight: 8.71 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O00560 (Residues: 197-273; Coverage: 26%)
Gene names: MDA9, SDCBP, SYCL
Sequence domains: PDZ domain
Structure domains: Pdz3 Domain

Ligands and Environments

1 bound ligand:
Ligand O 1 x O
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X9B
Spacegroup: P21
Unit cell:
a: 25.292Å b: 42.57Å c: 31.038Å
α: 90° β: 108.71° γ: 90°
R-values:
R R work R free
0.115 0.113 0.153
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Plasticity of PDZ domains in ligand recognition and signaling.
Ivarsson Y. (2012)
9 more

6 mentions without citation

Thermodynamic basis for promiscuity and selectivity in protein-protein interactions: PDZ domains, a case study.
Basdevant et al. (2006)
5 more