1BVN

PIG PANCREATIC ALPHA-AMYLASE IN COMPLEX WITH THE PROTEINACEOUS INHIBITOR TENDAMISTAT

Functional Information from GO Data

Chain	GOid	namespace	contents
P	0003824	molecular_function	catalytic activity
P	0004556	molecular_function	alpha-amylase activity
P	0005509	molecular_function	calcium ion binding
P	0005576	cellular_component	extracellular region
P	0005615	cellular_component	extracellular space
P	0005975	biological_process	carbohydrate metabolic process
P	0016052	biological_process	carbohydrate catabolic process
P	0016160	molecular_function	amylase activity
P	0016787	molecular_function	hydrolase activity
P	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
P	0031404	molecular_function	chloride ion binding
P	0043169	molecular_function	cation binding
P	0046872	molecular_function	metal ion binding
T	0015066	molecular_function	alpha-amylase inhibitor activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA P 2001

Chain	Residue
P	ASN100
P	ARG158
P	ASP167
P	HIS201
P	HOH1152

---

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL P 2002

Chain	Residue
P	ARG195
P	ARG337

---

site_id	AS
Number of Residues	3
Details	CATALYTICALLY ACTIVE RESIDUES.

Chain	Residue
P	ASP197
P	GLU233
P	ASP300

---

site_id	CA
Number of Residues	4
Details	CALCIUM BINDING SITE.

Chain	Residue
P	ASN100
P	ARG158
P	ASP167
P	HIS201

---

site_id	CL
Number of Residues	3
Details	CHLORIDE BINDING SITE.

Chain	Residue
P	ARG337
P	ARG195
P	ASN298

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Nucleophile"}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Proton donor"}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11412124","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11960990","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7897663","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8193143","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8681972","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8757803","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8994970","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9385631","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11412124","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11960990","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7897663","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8757803","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9385631","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Site: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P04746","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Pyrrolidone carboxylic acid","evidences":[{"source":"UniProtKB","id":"P04746","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine"}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1amy

Chain	Residue	Details
P	ASP300
P	ASP197
P	GLU233

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1amy

Chain	Residue	Details
P	ASP197
P	GLU233

---

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1amy

Chain	Residue	Details
P	ASP236
P	ASP197

---