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1VIW

TENEBRIO MOLITOR ALPHA-AMYLASE-INHIBITOR COMPLEX

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004556molecular_functionalpha-amylase activity
A0005509molecular_functioncalcium ion binding
A0005975biological_processcarbohydrate metabolic process
A0016052biological_processcarbohydrate catabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0031404molecular_functionchloride ion binding
A0043169molecular_functioncation binding
A0046872molecular_functionmetal ion binding
B0015066molecular_functionalpha-amylase inhibitor activity
B0030246molecular_functioncarbohydrate binding
Functional Information from PDB Data
site_idCIC
Number of Residues3
DetailsBINDING SITE
ChainResidue
AASP185
AGLU222
AASP287

Functional Information from PROSITE/UniProt
site_idPS00307
Number of Residues7
DetailsLECTIN_LEGUME_BETA Legume lectins beta-chain signature. VTVEFDT
ChainResidueDetails
BVAL98-THR104

site_idPS00308
Number of Residues10
DetailsLECTIN_LEGUME_ALPHA Legume lectins alpha-chain signature. VYDWVSVGFS
ChainResidueDetails
BVAL171-SER180

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues17
DetailsCompositional bias: {"description":"Polar residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"9600843","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"9600843","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10508777","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9600843","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9687373","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1JAE","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P04746","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"10100643","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP185
AGLY210

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP287
AASP185
AGLU222

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP287
AASP185
AGLU229

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PDB entries from 2026-01-14

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