CRYSTAL STRUCTURE OF A NEW ALKALINE SERINE PROTEASE (M-PROTEASE) FROM BACILLUS SP. KSM-K16CRYSTAL STRUCTURE OF A NEW ALKALINE SERINE PROTEASE (M-PROTEASE) FROM BACILLUS SP. KSM-K16

Structural highlights

1mpt is a 1 chain structure with sequence from Alkalihalobacillus clausii KSM-K16. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PRTM_ALKCK Alkaline serine protease that cleaves various substrates, including N-succinyl-Ala-Ala-Pro-Phe-pNA, N-succinyl-Ala-Ala-Pro-MetpNA, oxidized insulin B chain, casein, hemoglobin and scleroproteins, such as keratin, alpha-keratin and elastin.[1]

Evolutionary Conservation

 

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. Kobayashi T, Hakamada Y, Adachi S, Hitomi J, Yoshimatsu T, Koike K, Kawai S, Ito S. Purification and properties of an alkaline protease from alkalophilic Bacillus sp. KSM-K16. Appl Microbiol Biotechnol. 1995 Jul;43(3):473-81. PMID:7632397 doi:10.1007/BF00218452

1mpt, resolution 2.40Å

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