› 1d5g

Solution NMR

SOLUTION STRUCTURE OF THE PDZ2 DOMAIN FROM HUMAN PHOSPHATASE HPTP1E COMPLEXED WITH A PEPTIDE

Released:
DOI: 10.2210/pdb1d5g/pdb
PDB entry 1d5g coloured by chain, ensemble of 20 models, front view.
PDB entry 1d5g coloured by chain, ensemble of 20 models, side view.
PDB entry 1d5g coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Solution structure of the PDZ2 domain from cytosolic human phosphatase hPTP1E complexed with a peptide reveals contribution of the beta2-beta3 loop to PDZ domain-ligand interactions.
Kozlov G, Banville D, Gehring K, Ekiel I
J Mol Biol 320 813-20 (2002)
PMID: 12095257

Function and Biology Details

Reaction catalysed: 
Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-162152 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Tyrosine-protein phosphatase non-receptor type 13 Chain: A
Molecule details ›
Chain: A
Length: 96 amino acids
Theoretical weight: 10.02 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q12923 (Residues: 1361-1456; Coverage: 4%)
Gene names: PNP1, PTP1E, PTPL1, PTPN13
Sequence domains: PDZ domain
Structure domains: Pdz3 Domain
PEPTIDE FADSEADENEQVSAV Chain: B
Molecule details ›
Chain: B
Length: 15 amino acids
Theoretical weight: 1.61 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

3 review citations

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

16 mentions without citation

The origin of allosteric functional modulation: multiple pre-existing pathways.
del Sol et al. (2009)
15 more