› 4amh

X-ray diffraction
2.3Å resolution

Influence of circular permutation on the folding pathway of a PDZ domain

Released:
DOI: 10.2210/pdb4amh/pdb
PDB entry 4amh coloured by chain, front view.
PDB entry 4amh coloured by chain, side view.
PDB entry 4amh coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Tolerance of protein folding to a circular permutation in a PDZ domain.
Hultqvist G, Punekar AS, Morrone A, Chi CN, Engström A, Selmer M, Gianni S, Jemth P
PLoS One 7 e50055 (2012)
PMID: 23185531

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171456 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Disks large homolog 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 106 amino acids
Theoretical weight: 11.37 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q12959 (Residues: 327-405; Coverage: 9%)
Gene name: DLG1
Sequence domains: PDZ domain
Structure domains: Pdz3 Domain

Ligands and Environments

2 bound ligands:
Ligand TRS 1 x TRS
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: C2
Unit cell:
a: 106.9Å b: 43.6Å c: 51.7Å
α: 90° β: 103.7° γ: 90°
R-values:
R R work R free
0.222 0.22 0.268
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Specificity in PDZ-peptide interaction networks: Computational analysis and review.
Amacher et al. (2020)
1 more

1 mention without citation

Tolerance of protein folding to a circular permutation in a PDZ domain.
Hultqvist et al. (2012)