1T1G

High Resolution Crystal Structure of Mutant E23A of Kumamolisin, a sedolisin type proteinase (previously called Kumamolysin or KSCP)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004252	molecular_function	serine-type endopeptidase activity
A	0006508	biological_process	proteolysis
A	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 A 365

Chain	Residue
A	ASP316
A	ILE317
A	GLY334
A	GLY336
A	ASP338
A	HOH368

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site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 A 366

Chain	Residue
A	ARG201
A	PRO228
A	SER229
A	HOH407
A	HOH518
A	HOH569
A	SER198
A	ALA199
A	GLY200

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site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 A 367

Chain	Residue
A	LYS121
A	ARG327
A	ARG329
A	HOH389
A	HOH463
A	HOH532
A	HOH539
A	HOH575

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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
A	SER278
A	ASP164
A	ASP82
A	GLU78

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