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1JAE

STRUCTURE OF TENEBRIO MOLITOR LARVAL ALPHA-AMYLASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004556molecular_functionalpha-amylase activity
A0005509molecular_functioncalcium ion binding
A0005615cellular_componentextracellular space
A0005975biological_processcarbohydrate metabolic process
A0008152biological_processmetabolic 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
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 500
ChainResidue
AASN98
AARG146
AASP155
AHIS189
AHOH510
AHOH520
AHOH529

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 501
ChainResidue
AASN285
AARG321
AHOH521
AARG183
ALEU243

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:9600843
ChainResidueDetails
AASP185

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:9600843
ChainResidueDetails
AGLU222

site_idSWS_FT_FI3
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:10508777, ECO:0000269|PubMed:9600843, ECO:0000269|PubMed:9687373, ECO:0007744|PDB:1JAE
ChainResidueDetails
AASN98
AARG146
AASP155
AARG183
AHIS189
AASN285
AARG321

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000250|UniProtKB:P04746
ChainResidueDetails
AASP287

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:9199514, ECO:0000269|PubMed:9687373
ChainResidueDetails
APCA1

218853

PDB entries from 2024-04-24

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