1arb Summary

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THE PRIMARY STRUCTURE AND STRUCTURAL CHARACTERISTICS OF ACHROMOBACTER LYTICUS PROTEASE I, A LYSINE-SPECIFIC SERINE PROTEASE

The structure was published by Tsunasawa, S., Masaki, T., Hirose, M., Soejima, M., and Sakiyama, F., in 1989 in a paper entitled "The primary structure and structural characteristics of Achromobacter lyticus protease I, a lysine-specific serine protease." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.2 Å and deposited in 1993.

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

The PDB entry contains the structure of ACHROMOBACTER PROTEASE I. This molecule has the UniProt identifier P15636 (API_ACHLY)search. The sample contained 268 residues which is < 90% of the natural sequence. Out of 268 residues 263 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 ACHROMOBACTER PROTEASE I P15636 (206-473) (API_ACHLY)search Achromobacter lyticussearch < 90% 268 98%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P15636 (206 - 473) ACHROMOBACTER PROTEASE I Achromobacter lyticus

Chain Structural classification (SCOP) Structural classification (CATH)
A Prokaryotic proteasessearch Trypsin-like serine proteasessearch

Chain ID Molecular function (GO) Biological process (GO)
A (P15636) catalytic activitysearch serine-type endopeptidase activitysearch proteolysissearch

Chain InterPro annotation
A Peptidase S1search Trypsin-like cysteine/serine peptidase domainsearch