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1BG9

BARLEY ALPHA-AMYLASE WITH SUBSTRATE ANALOGUE ACARBOSE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004556molecular_functionalpha-amylase activity
A0005509molecular_functioncalcium ion binding
A0005975biological_processcarbohydrate metabolic process
A0005983biological_processstarch catabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0043169molecular_functioncation binding
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAS
Number of Residues3
Details
ChainResidue
AASP179
AGLU204
AASP289

site_idSS
Number of Residues2
Details
ChainResidue
ATRP276
ATRP277

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:9571044
ChainResidueDetails
AASP179

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:9571044
ChainResidueDetails
AGLU204

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000305|PubMed:9571044
ChainResidueDetails
ATYR51
AARG177
ATRP206
ASER208
AGLN226
AASP233
AGLY275
AHIS288

site_idSWS_FT_FI4
Number of Residues13
DetailsBINDING: BINDING => ECO:0000269|PubMed:8196040, ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702, ECO:0007744|PDB:1AVA
ChainResidueDetails
AASN91
APHE143
AALA146
AASP148
AGLY183
AGLU108
ATHR111
AASP113
AASP117
AASP127
AASP138
AALA141
AASP142

site_idSWS_FT_FI5
Number of Residues5
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00693
ChainResidueDetails
ALYS269
AGLN294
ALYS373
AVAL390
ATRP400

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000305|PubMed:9571044
ChainResidueDetails
AASP289

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP179
AGLU204

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP179
AASP233

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP179
AGLU204
ATRP206
AASP289

site_idCSA4
Number of Residues5
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AGLU204
AASP179
AARG177
AASP289
AHIS288

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AGLU204
AASP179
AHIS92
AASP289

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP179
AGLU204
AASP289

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP179
AASP289
AGLU227

site_idMCSA1
Number of Residues3
DetailsM-CSA 397
ChainResidueDetails
AASP179covalent catalysis
AGLU204hydrogen radical acceptor, proton shuttle (general acid/base)
AASP289electrostatic stabiliser, hydrogen radical acceptor, proton shuttle (general acid/base)

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PDB entries from 2024-07-24

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