CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN CARBOXYPEPTIDASE A AND THE BIPRODUCT ANALOG INHIBITOR L-BENZYLSUCCINATE AT 2.0 ANGSTROMS RESOLUTION
The structure was published by Mangani, S., Carloni, P., and Orioli, P., in 1992 in a paper entitled "Crystal structure of the complex between carboxypeptidase A and the biproduct analog inhibitor L-benzylsuccinate at 2.0 A resolution." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 1991.
The experimental data on which the structure is based was not deposited.
The PDB entry contains the structure of CARBOXYPEPTIDASE A. This molecule has the UniProt identifier P00730 (CBPA1_BOVIN). The sample contained 307 residues which is < 90% of the natural sequence. Out of 307 residues 307 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):
This entry contains 1 unique UniProt protein: