› 4uu5

X-ray diffraction
1.23Å resolution

CRYSTAL STRUCTURE OF THE PDZ DOMAIN OF PALS1 IN COMPLEX WITH THE CRB PEPTIDE

Released:
DOI: 10.2210/pdb4uu5/pdb
PDB entry 4uu5 coloured by chain, front view.
PDB entry 4uu5 coloured by chain, side view.
PDB entry 4uu5 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of the human Pals1 PDZ domain with and without ligand suggest gated access of Crb to the PDZ peptide-binding groove.
Ivanova ME, Fletcher GC, O'Reilly N, Purkiss AG, Thompson BJ, McDonald NQ
OpenAccess logo Acta Crystallogr D Biol Crystallogr 71 555-64 (2015)
PMID: 25760605

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-551091 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Protein PALS1 Chain: A
Molecule details ›
Chain: A
Length: 90 amino acids
Theoretical weight: 9.65 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q8N3R9 (Residues: 251-335; Coverage: 13%)
Gene names: MPP5, PALS1
Sequence domains: PDZ domain
Structure domains: Pdz3 Domain
Protein crumbs homolog 1 Chain: B
Molecule details ›
Chain: B
Length: 17 amino acids
Theoretical weight: 2.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P82279 (Residues: 1390-1406; Coverage: 1%)
Gene name: CRB1

Ligands and Environments

3 bound ligands:
Ligand CL 8 x CL
Ligand NA 1 x NA
Ligand PUN 1 x PUN
1 modified residue:
Ligand SME 1 x SME

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P4122
Unit cell:
a: 74.73Å b: 74.73Å c: 42.71Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 0.168 0.183
Expression system: Escherichia coli BL21

Quick links

Citations

2 review citations

Structural Features of Tight-Junction Proteins.
Heinemann et al. (2019)
1 more

10 mentions without citation

Synthetic Protein Scaffolds Based on Peptide Motifs and Cognate Adaptor Domains for Improving Metabolic Productivity.
Horn et al. (2015)
9 more