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3IJ9

Directed 'in situ' Elongation as a Strategy to Characterize the Covalent Glycosyl-Enzyme Catalytic Intermediate of Human Pancreatic a-Amylase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004556molecular_functionalpha-amylase activity
A0005509molecular_functioncalcium ion binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005975biological_processcarbohydrate metabolic process
A0016052biological_processcarbohydrate catabolic process
A0016160molecular_functionamylase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0031404molecular_functionchloride ion binding
A0043169molecular_functioncation binding
A0044245biological_processpolysaccharide digestion
A0046872molecular_functionmetal ion binding
A0070062cellular_componentextracellular exosome
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:10091666, ECO:0000305|PubMed:10769135, ECO:0000305|PubMed:11914097
ChainResidueDetails
AASP197

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:10091666, ECO:0000305|PubMed:10769135, ECO:0000305|PubMed:11772019, ECO:0000305|PubMed:11914097
ChainResidueDetails
AGLU233

site_idSWS_FT_FI3
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:10091666, ECO:0000269|PubMed:10769135, ECO:0000269|PubMed:11772019, ECO:0000269|PubMed:8528071, ECO:0007744|PDB:1HNY
ChainResidueDetails
AASN100
AARG158
AASP167
AARG195
AHIS201
AASN298
AARG337

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000305|PubMed:10091666, ECO:0000305|PubMed:10769135, ECO:0000305|PubMed:11914097
ChainResidueDetails
AASP300

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:11772019, ECO:0000269|PubMed:8528071
ChainResidueDetails
APCA1

site_idSWS_FT_FI6
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10091666, ECO:0000269|PubMed:10769135, ECO:0000269|PubMed:11772019
ChainResidueDetails
AASN461

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP300
AASP197
AGLU233

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP197
AGLU233

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP236
AASP197

227344

PDB entries from 2024-11-13

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