› 2f21

X-ray diffraction
1.5Å resolution

human Pin1 Fip mutant

Released:
DOI: 10.2210/pdb2f21/pdb
PDB entry 2f21 coloured by chain, front view.
PDB entry 2f21 coloured by chain, side view.
PDB entry 2f21 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure-function-folding relationship in a WW domain.
Jäger M, Zhang Y, Bieschke J, Nguyen H, Dendle M, Bowman ME, Noel JP, Gruebele M, Kelly JW
Proc Natl Acad Sci U S A 103 10648-53 (2006)
PMID: 16807295

Function and Biology Details

Reaction catalysed: 
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure 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: 162 amino acids
Theoretical weight: 18.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q13526 (Residues: 1-163; Coverage: 99%)
Gene name: PIN1
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand 1PE 2 x 1PE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P43212
Unit cell:
a: 49.012Å b: 49.012Å c: 135.278Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.227 0.226 0.248
Expression system: Escherichia coli

Quick links

Citations

17 review citations

Transition networks for modeling the kinetics of conformational change in macromolecules.
Noé et al. (2008)
16 more

33 mentions without citation

Fast protein folding kinetics.
Gelman et al. (2014)
32 more