4cms Summary

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X-RAY ANALYSES OF ASPARTIC PROTEINASES IV. STRUCTURE AND REFINEMENT AT 2.2 ANGSTROMS RESOLUTION OF BOVINE CHYMOSIN

The structure was published by Newman, M., Safro, M., Frazao, C., et al., Tickle, I.J., Blundell, T.L., and Andreeva, N., in 1991 in a paper entitled "X-ray analyses of aspartic proteinases. IV. Structure and refinement at 2.2 A resolution of bovine chymosin." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.2 Å and deposited in 1991.

The experimental data on which the structure is based was not deposited.

The PDB entry contains the structure of CHYMOSIN B. This molecule has the UniProt identifier P00794 (CHYM_BOVIN)search. The sample contained 323 residues which is < 90% of the natural sequence. Out of 323 residues 320 were observed and are deposited in the PDB.

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 CHYMOSIN B P00794 (59-381) (CHYM_BOVIN)search Bos taurussearch < 90% 323 99%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P00794 (59 - 381) CHYMOSIN B Bos taurus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A Pepsin-likesearch Acid Proteasessearch Eukaryotic aspartyl proteasesearch

Chain ID Molecular function (GO) Biological process (GO)
A (P00794) aspartic-type endopeptidase activitysearch proteolysissearch

Chain InterPro annotation
A Aspartic peptidasesearch Aspartic peptidase, active sitesearch Aspartic peptidase domainsearch