› 2qt5

X-ray diffraction
2.3Å resolution

Crystal Structure of GRIP1 PDZ12 in Complex with the Fras1 Peptide

Released:
DOI: 10.2210/pdb2qt5/pdb
PDB entry 2qt5 coloured by chain, front view.
PDB entry 2qt5 coloured by chain, side view.
PDB entry 2qt5 coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Supramodular nature of GRIP1 revealed by the structure of its PDZ12 tandem in complex with the carboxyl tail of Fras1.
Long J, Wei Z, Feng W, Yu C, Zhao YX, Zhang M
J Mol Biol 375 1457-68 (2008)
PMID: 18155042

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-161336 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Glutamate receptor-interacting protein 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 200 amino acids
Theoretical weight: 21.49 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P97879 (Residues: 48-243; Coverage: 18%)
Gene name: Grip1
Sequence domains: PDZ domain
Structure domains: Pdz3 Domain
(ASN)(ASN)(LEU)(GLN)(ASP)(GLY)(THR)(GLU)(VAL) Chains: X, Y
Molecule details ›
Chains: X, Y
Length: 9 amino acids
Theoretical weight: 989 Da
Source organism: Rattus norvegicus
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand EDO 2 x EDO
Ligand ACY 2 x ACY
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P212121
Unit cell:
a: 59.1Å b: 75.925Å c: 126.38Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.199 0.247
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

3 review citations

Organization and dynamics of PDZ-domain-related supramodules in the postsynaptic density.
Feng et al. (2009)
2 more

5 mentions without citation

PDZ domains and their binding partners: structure, specificity, and modification.
Lee et al. (2010)
4 more