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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7P32

Crystal structure of human lysosomal acid-alpha-glucosidase, GAA, in complex with cyclosulfamidate 6

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
AAA0000023biological_processmaltose metabolic process
AAA0002086biological_processdiaphragm contraction
AAA0003824molecular_functioncatalytic activity
AAA0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
AAA0004558molecular_functionalpha-1,4-glucosidase activity
AAA0005764cellular_componentlysosome
AAA0005765cellular_componentlysosomal membrane
AAA0005886cellular_componentplasma membrane
AAA0005975biological_processcarbohydrate metabolic process
AAA0005980biological_processglycogen catabolic process
AAA0005984biological_processdisaccharide metabolic process
AAA0005985biological_processsucrose metabolic process
AAA0006006biological_processglucose metabolic process
AAA0007040biological_processlysosome organization
AAA0016020cellular_componentmembrane
AAA0016787molecular_functionhydrolase activity
AAA0016798molecular_functionhydrolase activity, acting on glycosyl bonds
AAA0030246molecular_functioncarbohydrate binding
AAA0035577cellular_componentazurophil granule membrane
AAA0043202cellular_componentlysosomal lumen
AAA0043896molecular_functionglucan 1,6-alpha-glucosidase activity
AAA0061723biological_processglycophagy
AAA0070062cellular_componentextracellular exosome
AAA0070821cellular_componenttertiary granule membrane
AAA0090599molecular_functionalpha-glucosidase activity
AAA0101003cellular_componentficolin-1-rich granule membrane
AAA0120282cellular_componentautolysosome lumen
Functional Information from PROSITE/UniProt
site_idPS00025
Number of Residues22
DetailsP_TREFOIL_1 P-type 'Trefoil' domain signature. RfdCaPdkaiTqeqCeargCCY
ChainResidueDetails
AAAARG89-TYR110
site_idPS00129
Number of Residues8
DetailsGLYCOSYL_HYDROL_F31_1 Glycosyl hydrolases family 31 active site. GMWiDMNE
ChainResidueDetails
AAAGLY514-GLU521
site_idPS00707
Number of Residues31
DetailsGLYCOSYL_HYDROL_F31_2 Glycosyl hydrolases family 31 signature 2. GADVCGFlgnTseeLCvRWtqLGAFyPFmRN
ChainResidueDetails
AAAGLY643-ASN673
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10066","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1856189","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29061980","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29061980","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29061980","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8435067","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2016","submissionDatabase":"PDB data bank","title":"The structure of human GAA: structural basis of Pompe disease.","authors":["Deming D.T.","Garman S.C."]}},{"source":"PDB","id":"5KZW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5NN3","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"29061980","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8435067","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2016","submissionDatabase":"PDB data bank","title":"The structure of human GAA: structural basis of Pompe disease.","authors":["Deming D.T.","Garman S.C."]}},{"source":"PDB","id":"5KZW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5NN3","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29061980","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8435067","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2016","submissionDatabase":"PDB data bank","title":"The structure of human GAA: structural basis of Pompe disease.","authors":["Deming D.T.","Garman S.C."]}},{"source":"PDB","id":"5KZW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5NN3","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12754519","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29061980","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8435067","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2016","submissionDatabase":"PDB data bank","title":"The structure of human GAA: structural basis of Pompe disease.","authors":["Deming D.T.","Garman S.C."]}},{"source":"PDB","id":"5KZW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5NN3","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8435067","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246704

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