5b3y

X-ray diffraction
1.9Å resolution

Crystal structure of hPin1 WW domain (5-23) fused with maltose-binding protein

Released:

Function and Biology Details

Reaction catalysed:
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-142565 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Maltose/maltodextrin-binding periplasmic protein; Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 Chain: A
Molecule details ›
Chain: A
Length: 390 amino acids
Theoretical weight: 42.95 KDa
Source organisms: Expression system: Escherichia coli
UniProt:
  • Canonical: Q13526 (Residues: 5-23; Coverage: 12%)
  • Canonical: P0AEX9 (Residues: 27-393; Coverage: 99%)
Gene names: JW3994, PIN1, b4034, malE
Sequence domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P212121
Unit cell:
a: 48.296Å b: 57.637Å c: 124.056Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 0.165 0.189
Expression system: Escherichia coli