› 5hed

X-ray diffraction
1.7Å resolution

The third PDZ domain from the synaptic protein PSD-95 in complex with a mutant C-terminal peptide derived from CRIPT (T-2F)

Released:
DOI: 10.2210/pdb5hed/pdb
PDB entry 5hed coloured by chain, front view.
PDB entry 5hed coloured by chain, side view.
PDB entry 5hed coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Origins of Allostery and Evolvability in Proteins: A Case Study.
Raman AS, White KI, Ranganathan R
Cell 166 468-480 (2016)
PMID: 27321669

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-151888 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Disks large homolog 4 Chain: A
Molecule details ›
Chain: A
Length: 119 amino acids
Theoretical weight: 12.74 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P31016 (Residues: 302-402; Coverage: 14%)
Gene names: Dlg4, Dlgh4, Psd95
Sequence domains: PDZ domain
Structure domains: Pdz3 Domain
Cysteine-rich PDZ-binding protein Chain: B
Molecule details ›
Chain: B
Length: 9 amino acids
Theoretical weight: 1.12 KDa
Source organism: Rattus norvegicus
Expression system: Not provided
UniProt:
  • Canonical: Q792Q4 (Residues: 93-101; Coverage: 9%)
Gene name: Cript

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: P4132
Unit cell:
a: 89.551Å b: 89.551Å c: 89.551Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.173 0.17 0.197
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

10 review citations

The causes of evolvability and their evolution.
Payne et al. (2019)
9 more