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1BLI

BACILLUS LICHENIFORMIS ALPHA-AMYLASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004556molecular_functionalpha-amylase activity
A0005509molecular_functioncalcium ion binding
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 500
ChainResidue
AASP161
AALA181
AASP183
AASP202
AASP204
AHOH2079

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 600
ChainResidue
AASN104
AASP194
AASP200
AHIS235
AHOH2080

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 700
ChainResidue
AGLY300
ATYR302
AHIS406
AASP407
AASP430
AHOH2069

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 800
ChainResidue
AASP161
AASP183
AASP194
AASP200
AILE201

site_idCA1
Number of Residues4
DetailsCALCIUM BINDING SITE. THIS CALCIUM BINDING SITE IS CONSERVED IN ALL STRUCTURES OF ALPHA-AMYLASES AND RELATED ENZYMES.
ChainResidue
AASN104
AASP194
AASP200
AHIS235

site_idCA2
Number of Residues5
DetailsCALCIUM BINDING SITE. THIS CALCIUM BINDING SITE IS NOT CONSERVED IN ALL STRUCTURES OF ALPHA-AMYLASES AND RELATED ENZYMES.
ChainResidue
AASP183
AASP202
AASP204
AASP161
AALA181

site_idCA3
Number of Residues5
DetailsCALCIUM BINDING SITE. THIS CALCIUM BINDING SITE LOCATED IN THE INTERFACE BETWEEN DOMAIN A AND C IS NOT CONSERVED IN ALL STRUCTURES OF ALPHA-AMYLASES AND RELATED ENZYMES.
ChainResidue
AGLY300
ATYR302
AHIS406
AASP407
AASP430

site_idCS
Number of Residues3
DetailsCATALYTIC SITE.
ChainResidue
AMET197
AVAL233
AGLY300

site_idNA1
Number of Residues5
DetailsSODIUM BINDING SITE. THIS IS THE FIRST SODIUM BINDING SITE OBSERVED IN AN ALPHA-AMYLASE OR RELATED ENZYME. THIS SODIUM TOGETHER WITH THE CALCIUM IONS CA1 AND CA2 FORM A LINEAR TRIADIC ARRAY WITH THE CALCIUM IONS 4.1 AND 4.5 A FROM THE CENTRAL SODIUM ION.
ChainResidue
AASP161
AASP183
AASP194
AASP200
AILE201

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile
ChainResidueDetails
AASP231

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor
ChainResidueDetails
AGLU261

site_idSWS_FT_FI3
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551, ECO:0007744|PDB:1BLI, ECO:0007744|PDB:1OB0
ChainResidueDetails
AASN104
AALA181
AASP202
AASP204
AGLY300
ATYR302
AHIS406
AASP407
AASP430

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551
ChainResidueDetails
AASP161
AASP183
AASP194
AASP200

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0007744|PDB:1BLI, ECO:0007744|PDB:1OB0
ChainResidueDetails
AHIS235

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000250
ChainResidueDetails
AASP328

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP328
AASP231
AGLU261
AHIS105

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP328
AASP231
AGLU261

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP231
AGLU261

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP231
AASP328
ATRP263
AGLU261

site_idCSA5
Number of Residues5
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP231
AASP328
AARG229
AGLU261
AHIS327

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PDB entries from 2024-07-24

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