5b3w

X-ray diffraction
2.4Å resolution

Crystal structure of hPin1 WW domain (5-15) fused with maltose-binding protein in C2221 form

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 382 amino acids
Theoretical weight: 42.05 KDa
Source organisms: Expression system: Escherichia coli
UniProt:
  • Canonical: Q13526 (Residues: 5-15; Coverage: 7%)
  • Canonical: P0AEX9 (Residues: 27-393; Coverage: 99%)
Gene names: JW3994, PIN1, b4034, malE
Sequence domains: Bacterial extracellular solute-binding protein

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: C2221
Unit cell:
a: 97.525Å b: 126.103Å c: 173.523Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.173 0.171 0.214
Expression system: Escherichia coli