1GTG

Crystal structure of the thermostable serine-carboxyl type proteinase, kumamolysin (kscp)

Functional Information from GO Data

Chain	GOid	namespace	contents
1	0004252	molecular_function	serine-type endopeptidase activity
1	0006508	biological_process	proteolysis
1	0008236	molecular_function	serine-type peptidase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA 11371

Chain	Residue
1	ASP316
1	ILE317
1	GLY334
1	GLY336
1	ASP338
1	HOH2152

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"12057200","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15242607","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	5
Details	Binding 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"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1nlu

Chain	Residue	Details
1	SER278
1	ASP164
1	ASP82
1	GLU78

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