1BG9

BARLEY ALPHA-AMYLASE WITH SUBSTRATE ANALOGUE ACARBOSE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004556	molecular_function	alpha-amylase activity
A	0005509	molecular_function	calcium ion binding
A	0005975	biological_process	carbohydrate metabolic process
A	0005983	biological_process	starch catabolic process
A	0008152	biological_process	metabolic process
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0043169	molecular_function	cation binding
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AS
Number of Residues	3
Details

Chain	Residue
A	ASP179
A	GLU204
A	ASP289

---

site_id	SS
Number of Residues	2
Details

Chain	Residue
A	TRP276
A	TRP277

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Nucleophile => ECO:0000305|PubMed:9571044

Chain	Residue	Details
A	ASP179

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000305|PubMed:9571044

Chain	Residue	Details
A	GLU204

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000305|PubMed:9571044

Chain	Residue	Details
A	TYR51
A	ARG177
A	TRP206
A	SER208
A	GLN226
A	ASP233
A	GLY275
A	HIS288

---

site_id	SWS_FT_FI4
Number of Residues	13
Details	BINDING: BINDING => ECO:0000269|PubMed:8196040, ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702, ECO:0007744|PDB:1AVA

Chain	Residue	Details
A	ASN91
A	PHE143
A	ALA146
A	ASP148
A	GLY183
A	GLU108
A	THR111
A	ASP113
A	ASP117
A	ASP127
A	ASP138
A	ALA141
A	ASP142

---

site_id	SWS_FT_FI5
Number of Residues	5
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P00693

Chain	Residue	Details
A	LYS269
A	GLN294
A	LYS373
A	VAL390
A	TRP400

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	SITE: Transition state stabilizer => ECO:0000305|PubMed:9571044

Chain	Residue	Details
A	ASP289

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 397

Chain	Residue	Details
A	ASP179	covalent catalysis
A	GLU204	hydrogen radical acceptor, proton shuttle (general acid/base)
A	ASP289	electrostatic stabiliser, hydrogen radical acceptor, proton shuttle (general acid/base)

---