1K9X: Structure Of Pyrococcus Furiosus Carboxypeptidase Apo-Yb

The structure of Pyrococcus furiosus carboxypeptidase (PfuCP) has been determined to 2.2 A resolution using multiwavelength anomalous diffraction (MAD) methods. PfuCP represents the first structure of the new M32 family of carboxypeptidases. The overall structure is comprised of a homodimer. Each subunit is mostly helical with its most pronounced feature being a deep substrate binding groove. The active site lies at the bottom of this groove and contains an HEXXH motif that coordinates the metal ion required for catalysis. Surprisingly, the structure is similar to the recently reported rat neurolysin. Comparison of these structures as well as sequence analyses with other homologous proteins reveal several conserved residues. The roles for these conserved residues in the catalytic mechanism are inferred based on modeling and their location.
PDB ID: 1K9XDownload
MMDB ID: 20860
PDB Deposition Date: 2001/10/31
Updated in MMDB: 2002/11
Experimental Method:
x-ray diffraction
Resolution: 2.3  Å
Source Organism:
Similar Structures:
Biological Unit for 1K9X: dimeric; determined by author and by software (PISA)
Molecular Components in 1K9X
Label Count Molecule
Proteins (2 molecules)
M32 Carboxypeptidase(Gene symbol: PF_RS02345)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB