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1T1E

High Resolution Crystal Structure of the Intact Pro-Kumamolisin, a Sedolisin Type Proteinase (previously called Kumamolysin or KSCP)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004175molecular_functionendopeptidase activity
A0004252molecular_functionserine-type endopeptidase activity
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008236molecular_functionserine-type peptidase activity
A0008240molecular_functiontripeptidyl-peptidase activity
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 700
ChainResidue
AASP505
AILE506
AGLY523
AGLY525
AASP527
AHOH701

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"12057200","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15242607","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12057200","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15242607","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1GT9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GTG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GTJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GTL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1T1E","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1T1G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1T1I","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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