› 5vti

X-ray diffraction
1.8Å resolution

Structure of Pin1 WW Domain Sequence 3 with [R,R]-ACPC Loop Substitution

Released:
DOI: 10.2210/pdb5vti/pdb
PDB entry 5vti coloured by chain, front view.
PDB entry 5vti coloured by chain, side view.
PDB entry 5vti coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Evaluation of β-Amino Acid Replacements in Protein Loops: Effects on Conformational Stability and Structure.
Mortenson DE, Kreitler DF, Thomas NC, Guzei IA, Gellman SH, Forest KT
Chembiochem 19 604-612 (2018)
PMID: 29272560

Function and Biology Details

Reaction catalysed: 
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171737 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 Chain: A
Molecule details ›
Chain: A
Length: 32 amino acids
Theoretical weight: 3.81 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q13526 (Residues: 6-39; Coverage: 20%)
Gene name: PIN1
Sequence domains: WW domain

Ligands and Environments

1 bound ligand:
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P43212
Unit cell:
a: 48.173Å b: 48.173Å c: 37.214Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.235 0.231 0.275
Expression system: Not provided

Quick links

Citations

2 review citations

Conformational landscape of substituted prolines.
Ganguly et al. (2020)
1 more

1 mention without citation

Evaluation of β-Amino Acid Replacements in Protein Loops: Effects on Conformational Stability and Structure.
Mortenson et al. (2018)