{"context":{"query":">>uniprot>>pdb","source_dataset":"uniprot","target_dataset":"pdb"},"stats":{"queried":1,"total":58,"mapped":1},"pagination":{"has_next":false},"schema":"id|title|method|resolution|source_organism|chain_count|header","mappings":[{"input":"P04062","source":"P04062|Lysosomal acid glucosylceramidase","targets":["1OGS|human acid-beta-glucosidase|X-RAY DIFFRACTION|2|Homo sapiens|0|HYDROLASE","1Y7V|X-ray structure of human acid-beta-glucosidase covalently bound to conduritol B epoxide|X-RAY DIFFRACTION|2.4|Homo sapiens|0|HYDROLASE","2F61|Crystal structure of partially deglycosylated acid beta-glucosidase|X-RAY DIFFRACTION|2.5|Homo sapiens|0|HYDROLASE","2J25|Partially deglycosylated glucoceramidase|X-RAY DIFFRACTION|2.9|HOMO SAPIENS|0|HYDROLASE","2NSX|Structure of acid-beta-glucosidase with pharmacological chaperone provides insight into Gaucher disease|X-RAY DIFFRACTION|2.11|Homo sapiens|0|HYDROLASE","2NT0|Acid-beta-glucosidase low pH, glycerol bound|X-RAY DIFFRACTION|1.79|Homo sapiens|0|HYDROLASE","2NT1|Structure of acid-beta-glucosidase at neutral pH|X-RAY DIFFRACTION|2.3|Homo sapiens|0|HYDROLASE","2V3D|acid-beta-glucosidase with N-butyl-deoxynojirimycin|X-RAY DIFFRACTION|1.96|HOMO SAPIENS|0|HYDROLASE","2V3E|acid-beta-glucosidase with N-nonyl-deoxynojirimycin|X-RAY DIFFRACTION|2|HOMO SAPIENS|0|HYDROLASE","2V3F|acid-beta-glucosidase produced in carrot|X-RAY DIFFRACTION|1.95|HOMO SAPIENS|0|HYDROLASE","2VT0|X-ray structure of a conjugate with conduritol-beta-epoxide of acid-beta-glucosidase overexpressed in cultured plant cells|X-RAY DIFFRACTION|2.15|HOMO SAPIENS|0|HYDROLASE","2WCG|X-ray structure of acid-beta-glucosidase with N-octyl(cyclic guanidine)-nojirimycin in the active site|X-RAY DIFFRACTION|2.3|HOMO SAPIENS|0|HYDROLASE","2WKL|Velaglucerase alfa|X-RAY DIFFRACTION|2.7|HOMO SAPIENS|0|HYDROLASE","2XWD|X-RAY STRUCTURE OF ACID-BETA-GLUCOSIDASE WITH 5N,6O-(N'-(N-OCTYL)IMINO)NOJIRIMYCIN IN THE ACTIVE SITE|X-RAY DIFFRACTION|2.66|HOMO SAPIENS|0|HYDROLASE","2XWE|X-RAY STRUCTURE OF ACID-BETA-GLUCOSIDASE WITH 5N,6S-(N'-(N-OCTYL)IMINO)-6-THIONOJIRIMYCIN IN THE ACTIVE SITE|X-RAY DIFFRACTION|2.31|HOMO SAPIENS|0|HYDROLASE","3GXD|Crystal structure of Apo acid-beta-glucosidase pH 4.5|X-RAY DIFFRACTION|2.5|Homo sapiens|0|HYDROLASE","3GXF|Crystal structure of acid-beta-glucosidase with isofagomine at neutral pH|X-RAY DIFFRACTION|2.4|Homo sapiens|0|HYDROLASE","3GXI|Crystal structure of acid-beta-glucosidase at pH 5.5|X-RAY DIFFRACTION|1.84|Homo sapiens|0|HYDROLASE","3GXM|Crystal structure of acid-beta-glucosidase at pH 4.5, phosphate crystallization condition|X-RAY DIFFRACTION|2.2|Homo sapiens|0|HYDROLASE","3KE0|Crystal structure of N370S Glucocerebrosidase at acidic pH.|X-RAY DIFFRACTION|2.7|Homo sapiens|0|HYDROLASE","3KEH|Crystal Structure of N370S Glucocerebrosidase mutant at pH 7.4|X-RAY DIFFRACTION|2.8|Homo sapiens|0|HYDROLASE","3RIK|The acid beta-glucosidase active site exhibits plasticity in binding 3,4,5,6-tetrahydroxyazepane-based inhibitors: implications for pharmacological chaperone design for gaucher disease|X-RAY DIFFRACTION|2.48|Homo sapiens|0|HYDROLASE/HYDROLASE INHIBITOR","3RIL|The acid beta-glucosidase active site exhibits plasticity in binding 3,4,5,6-tetrahydroxyazepane-based inhibitors: implications for pharmacological chaperone design for gaucher disease|X-RAY DIFFRACTION|2.4|Homo sapiens|0|HYDROLASE/HYDROLASE INHIBITOR","5LVX|Crystal structure of glucocerebrosidase with an inhibitory quinazoline modulator|X-RAY DIFFRACTION|2.2|Homo sapiens|0|HYDROLASE","6MOZ|Structure of acid-beta-glucosidase in complex with an aromatic pyrrolidine iminosugar inhibitor|X-RAY DIFFRACTION|2.1|Homo sapiens|0|HYDROLASE","6Q1N|Glucocerebrosidase in complex with pharmacological chaperone IMX8|X-RAY DIFFRACTION|2.526|Homo sapiens|0|HYDROLASE/INHIBITOR","6Q1P|Glucocerebrosidase in complex with pharmacological chaperone norIMX8|X-RAY DIFFRACTION|2.796|Homo sapiens|0|HYDROLASE/INHIBITOR","6Q6K|Crystal structure of recombinant human beta-glucocerebrosidase in complex with cyclophellitol activity based probe with Cy5 tag (ME569)|X-RAY DIFFRACTION|1.92|Homo sapiens|0|HYDROLASE","6Q6L|Crystal structure of recombinant human beta-glucocerebrosidase in complex with adamantyl-cyclophellitol inhibitor (ME656)|X-RAY DIFFRACTION|1.81|Homo sapiens|0|HYDROLASE","6Q6N|Crystal structure of recombinant human beta-glucocerebrosidase in complex with biphenyl-cyclophellitol inhibitor (ME655)|X-RAY DIFFRACTION|1.63|Homo sapiens|0|HYDROLASE","6T13|CRYSTAL STRUCTURE OF GLUCOCEREBROSIDASE IN COMPLEX WITH A PYRROLOPYRAZINE|X-RAY DIFFRACTION|1.85|Homo sapiens|0|HYDROLASE","6TJJ|Structure of Cerezyme at pH 4.6|X-RAY DIFFRACTION|1.59|Homo sapiens|0|HYDROLASE","6TJK|Crystal Structure of Recombinant GBA in Complex with Bis-Tris Propane.|X-RAY DIFFRACTION|1.56|Homo sapiens|0|HYDROLASE","6TJQ|Crystal Structure of Recombinant GBA in Complex with 2-Deoxy-2-fluoro-beta-D-glucopyranoside|X-RAY DIFFRACTION|1.41|Homo sapiens|0|HYDROLASE","6TN1|Unliganded Crystal Structure of Recombinant GBA|X-RAY DIFFRACTION|0.98|Homo sapiens|0|HYDROLASE","6YTP|Structure of recombinant human beta-glucocerebrosidase in complex with azide tagged cyclophellitol epoxide inhibitor|X-RAY DIFFRACTION|1.7|Homo sapiens|0|HYDROLASE","6YTR|Structure of recombinant human beta-glucocerebrosidase in complex with cyclophellitol aziridine inhibitor|X-RAY DIFFRACTION|1.7|Homo sapiens|0|HYDROLASE","6YUT|Structure of recombinant human beta-glucocerebrosidase in complex with N-acyl functionalised cyclophellitol aziridine|X-RAY DIFFRACTION|1.76|Homo sapiens|0|HYDROLASE","6YV3|Structure of recombinant human beta-glucocerebrosidase in complex with galacto-configured cyclophellitol aziridine inhibitor|X-RAY DIFFRACTION|1.8|Homo sapiens|0|HYDROLASE","6Z39|Structure of recombinant human beta-glucocerebrosidase in complex with BODIPY functionalised epoxide activity based probe|X-RAY DIFFRACTION|1.7|Homo sapiens|0|HYDROLASE","6Z3I|Structure of recombinant beta-glucocerebrosidase in complex with bifunctional cyclophellitol aziridine activity based probe|X-RAY DIFFRACTION|1.8|Homo sapiens|0|HYDROLASE","7NWV|Structure of recombinant human beta-glucocerebrosidase in complex with BODIPY Tagged Cyclophellitol activity based probe|X-RAY DIFFRACTION|1.86|Homo sapiens|0|HYDROLASE","8AWK|Structure of recombinant human beta-glucocerebrosidase in complex with D-carbaxylosyl chloride|X-RAY DIFFRACTION|1.58|Homo sapiens|0|HYDROLASE","8AWR|Structure of recombinant human beta-glucocerebrosidase in complex with L-carbaxylosyl chloride|X-RAY DIFFRACTION|1.49|Homo sapiens|0|HYDROLASE","8AX3|Structure of recombinant human beta-glucocerebrosidase in complex with L-carbaxylosyl fluoride|X-RAY DIFFRACTION|1.59|Homo sapiens|0|HYDROLASE","8P3E|Crystal structure of glucocerebrosidase in complex with allosteric activator|X-RAY DIFFRACTION|1.75|Homo sapiens|0|HYDROLASE","8P41|Crystal structure of glucocerebrosidase in complex with allosteric activator|X-RAY DIFFRACTION|1.83|Homo sapiens|0|HYDROLASE","9ENA|Lysosomal glucocerebrosidase in complex with a stabilizing nanobody|X-RAY DIFFRACTION|1.7|Homo sapiens; Lama glama|0|HYDROLASE","9F9Z|Gcase in complex with small molecule inhibitor 1|X-RAY DIFFRACTION|2.279|Homo sapiens|0|LIPID BINDING PROTEIN","9FA3|Gcase in complex with small molecule inhibitor 1|X-RAY DIFFRACTION|1.36|Homo sapiens|0|LIPID BINDING PROTEIN","9FA6|Gcase in complex with small molecule inhibitor 1|X-RAY DIFFRACTION|1.49|Homo sapiens|0|LIPID BINDING PROTEIN","9FAD|Gcase in complex with small molecule inhibitor 1|X-RAY DIFFRACTION|1.8|Homo sapiens|0|LIPID BINDING PROTEIN","9FAL|Gcase in complex with small molecule inhibitor 1|X-RAY DIFFRACTION|1.39|Homo sapiens|0|LIPID BINDING PROTEIN","9FAY|Gcase in complex with small molecule inhibitor 1|X-RAY DIFFRACTION|1.4|Homo sapiens|0|LIPID BINDING PROTEIN","9FAZ|Gcase in complex with small molecule inhibitor 1|X-RAY DIFFRACTION|1.63|Homo sapiens|0|LIPID BINDING PROTEIN","9FB2|Gcase in complex with small molecule inhibitor 1|X-RAY DIFFRACTION|1.14|Homo sapiens|0|LIPID BINDING PROTEIN","9FDI|Gcase in complex with small molecule inhibitor 1|X-RAY DIFFRACTION|1.41|Homo sapiens|0|LIPID BINDING PROTEIN","9FJF|Lysosomal transporting complex of beta-glucocerebrosidase (GCase) and lysosomal integral membrane protein 2 (LIMP-2) with bound Pro-macrobodies (Combined focus map)|ELECTRON MICROSCOPY|3.7|Homo sapiens; synthetic construct|0|TRANSPORT PROTEIN"]}]}