1gt9 Summary

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HIGH RESOLUTION CRYSTAL STRUCTURE OF A THERMOSTABLE SERINE-CARBOXYL TYPE PROTEINASE, KUMAMOLISIN (KSCP)

The structure was published by Comellas-Bigler, M., Fuentes-Prior, P., Maskos, K., et al., Dunn, B.M., Oda, K., and Bode, W., in 2002 in a paper entitled "The 1.4 A Crystal Structure of Kumamolysin. A Thermostable Serine-Carboxyl-Type Proteinase" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.38 Å and deposited in 2002.

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

This PDB entry contains multiple copies of the structure of KUMAMOLYSIN.

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 most likely forms homodimers.

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
1 KUMAMOLYSIN Q8RR56 (189-545) (Q8RR56_9BACI)search Bacillus sp. MN-32search 100% 357 100%
2 KUMAMOLYSIN Q8RR56 (189-545) (Q8RR56_9BACI)search Bacillus sp. MN-32search 100% 357 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q8RR56 (189 - 545) KUMAMOLYSIN Bacillus subtilis

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
1, 2 (Q8RR56) Serine-carboxyl proteinase, SCPsearch Rossmann foldsearch PF00082: Subtilase familysearch

Chain ID Molecular function (GO) Biological process (GO)
1, 2 (Q8RR56) serine-type endopeptidase activitysearch proteolysissearch

Chain InterPro annotation
1, 2 Peptidase S8/S53 domainsearch