1QHO

FIVE-DOMAIN ALPHA-AMYLASE FROM BACILLUS STEAROTHERMOPHILUS, MALTOSE/ACARBOSE COMPLEX

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004556	molecular_function	alpha-amylase activity
A	0005975	biological_process	carbohydrate metabolic process
A	0030246	molecular_function	carbohydrate binding
A	0043169	molecular_function	cation binding
A	2001070	molecular_function	starch binding

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P13507

Chain	Residue	Details
A	ASP228

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000250|UniProtKB:P13507

Chain	Residue	Details
A	GLU256

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site_id	SWS_FT_FI3
Number of Residues	15
Details	BINDING: BINDING => ECO:0000269|PubMed:10387084, ECO:0007744|PDB:1QHO

Chain	Residue	Details
A	ASP21
A	GLU101
A	GLU102
A	ASN131
A	GLN184
A	ASP198
A	HIS232
A	ASP23
A	ASN26
A	ASN27
A	GLY48
A	ASP50
A	ASP76
A	ASN77
A	ASP79

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site_id	SWS_FT_FI4
Number of Residues	7
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P0C1B3

Chain	Residue	Details
A	TRP93
A	HIS132
A	ARG226
A	LYS231
A	GLY259
A	ASP329
A	ARG376

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site_id	SWS_FT_FI5
Number of Residues	1
Details	SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P0C1B3

Chain	Residue	Details
A	ASP329

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details

Chain	Residue	Details
A	ASP228
A	ASP329
A	GLU256
A	HIS132

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site_id	MCSA1
Number of Residues	3
Details	M-CSA 905

Chain	Residue	Details
A	ASP228	covalent catalysis
A	GLU256	proton shuttle (general acid/base)
A	ASP329	transition state stabiliser

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