1m4l Summary



The structure was published by Kilshtain-Vardi, A., Glick, M., Greenblatt, H.M., Goldblum, A., and Shoham, G., in 2003 in a paper entitled "Refined structure of bovine carboxypeptidase A at 1.25 A resolution." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.25 Å and deposited in 2002.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of CARBOXYPEPTIDASE A. This molecule has the UniProt identifier P00730 (CBPA1_BOVIN)search. The sample contained 307 residues which is < 90% of the natural sequence. Out of 307 residues 306 were observed and are deposited in the PDB.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule is most likely monomeric.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A CARBOXYPEPTIDASE A P00730 (111-417) (CBPA1_BOVIN)search Bos taurussearch < 90% 307 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P00730 (111 - 417) CARBOXYPEPTIDASE A Bos taurus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A Pancreatic carboxypeptidasessearch Zn peptidasessearch Zinc carboxypeptidasesearch

Chain ID Molecular function (GO) Biological process (GO)
A (P00730) metallocarboxypeptidase activitysearch zinc ion bindingsearch proteolysissearch

Chain InterPro annotation
A Peptidase M14, carboxypeptidase Asearch