1WZK

Thermoactinomyces vulgaris R-47 alpha-amylase II (TVA II) mutatnt D465N

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
A	0005975	biological_process	carbohydrate metabolic process
A	0008152	biological_process	metabolic process
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0031216	molecular_function	neopullulanase activity
A	0046872	molecular_function	metal ion binding
B	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
B	0005975	biological_process	carbohydrate metabolic process
B	0008152	biological_process	metabolic process
B	0016787	molecular_function	hydrolase activity
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0031216	molecular_function	neopullulanase activity
B	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CA A 1601

Chain	Residue
A	ASN143
A	ASP145
A	ASN148
A	ASP149
A	GLY169
A	ASP171
A	HOH1666

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site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CA B 1602

Chain	Residue
B	ASN148
B	ASP149
B	GLY169
B	ASP171
B	HOH1669
B	ASN143
B	ASP145

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P38940

Chain	Residue	Details
A	ASP325
B	ASP325

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site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton donor => ECO:0000250|UniProtKB:P38940

Chain	Residue	Details
A	GLU354
B	GLU354

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site_id	SWS_FT_FI3
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269|PubMed:12051850, ECO:0007744|PDB:1JI2

Chain	Residue	Details
A	ASN143
B	ASP149
B	GLY169
B	ASP171
A	ASP145
A	ASN148
A	ASP149
A	GLY169
A	ASP171
B	ASN143
B	ASP145
B	ASN148

---

site_id	SWS_FT_FI4
Number of Residues	10
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P38940

Chain	Residue	Details
A	HIS244
B	ARG469
A	ARG323
A	HIS420
A	ASN465
A	ARG469
B	HIS244
B	ARG323
B	HIS420
B	ASN465

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site_id	SWS_FT_FI5
Number of Residues	2
Details	SITE: Transition state stabilizer => ECO:0000250

Chain	Residue	Details
A	ASP421
B	ASP421

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 433

Chain	Residue	Details
A	ASP325	covalent catalysis
A	GLU354	proton shuttle (general acid/base)
A	ASP421	transition state stabiliser

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site_id	MCSA2
Number of Residues	3
Details	M-CSA 433

Chain	Residue	Details
B	ASP325	covalent catalysis
B	GLU354	proton shuttle (general acid/base)
B	ASP421	transition state stabiliser

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