1ZVK

Structure of Double mutant, D164N, E78H of Kumamolisin-As

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
B	0004252	molecular_function	serine-type endopeptidase activity
B	0006508	biological_process	proteolysis
B	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 501

Chain	Residue
A	ASP316
A	ILE317
A	GLY334
A	GLY336
A	ASP338
A	HOH1001

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 502

Chain	Residue
B	GLY336
B	ASP338
B	HOH2001
B	ASP316
B	ILE317
B	GLY334

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	706
Details	Domain: {"description":"Peptidase S53","evidences":[{"source":"PROSITE-ProRule","id":"PRU01032","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	6
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"15014068","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16704427","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15014068","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16704427","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1SIO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SIU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SN7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ZVJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ZVK","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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