› 3qjm

X-ray diffraction
2.31Å resolution

Structural flexibility of Shank PDZ domain is important for its binding to different ligands

Released:
DOI: 10.2210/pdb3qjm/pdb
PDB entry 3qjm coloured by chain, front view.
PDB entry 3qjm coloured by chain, side view.
PDB entry 3qjm coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
The structural flexibility of the shank1 PDZ domain is important for its binding to different ligands.
Lee JH, Park H, Park SJ, Kim HJ, Eom SH
Biochem Biophys Res Commun 407 207-12 (2011)
PMID: 21376703

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-163939 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
SH3 and multiple ankyrin repeat domains protein 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 115 amino acids
Theoretical weight: 12.76 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WV48 (Residues: 654-768; Coverage: 5%)
Gene name: Shank1
Sequence domains: PDZ domain
Structure domains: Pdz3 Domain
Beta-PIX Chains: C, D
Molecule details ›
Chains: C, D
Length: 5 amino acids
Theoretical weight: 591 Da
Source organism: Rattus norvegicus
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P41212
Unit cell:
a: 57.625Å b: 57.625Å c: 144.042Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.236 0.235 0.267
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

1 review citation

Plasticity of PDZ domains in ligand recognition and signaling.
Ivarsson Y. (2012)
12 other articles

3 mentions without citation

Stereochemical determinants of C-terminal specificity in PDZ peptide-binding domains: a novel contribution of the carboxylate-binding loop.
Amacher et al. (2013)
2 more