2NUL: PEPTIDYLPROLYL ISOMERASE FROM E. COLI

Citation:
Abstract
The structure of the unliganded form of the Escherichia coli cytoplasmic peptidyl-prolyl isomerase (ppiB gene product) in a new crystal form was determined by the molecular replacement method and refined to an R-factor of 16.1% at 2.1 A resolution. The enzyme crystallized in the orthorhombic C2221 space group with unit cell dimensions of a=44.7 A, b=68.2 A and c=102.0 A. Comparison with the reported structure of the enzyme complexed with the tripeptide substrate succinyl-Ala-Pro-Ala-p-nitroanilide revealed subtle changes that occur upon complex formation. There is evidence to suggest that two surface loops have significantly reduced mobility in the complexed structure.
PDB ID: 2NULDownload
MMDB ID: 58133
PDB Deposition Date: 1996/11/14
Updated in MMDB: 2011/11
Experimental Method:
x-ray diffraction
Resolution: 2.1  Å
Source Organism:
Similar Structures:
Biological Unit for 2NUL: dimeric; determined by author
Molecular Components in 2NUL
Label Count Molecule
Proteins (2 molecules)
2
Peptidylprolyl Isomerase(Gene symbol: ppiB)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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