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DESCRIBE <http://purl.uniprot.org/SHA-384/4CDB6954ADDD028C88780C7F91644AE79E28738FC002F04C49B1FDF2EC8C3C899C1087A90336A6E67D2E8551955EEE31>
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http://purl.uniprot.org/SHA-384/4CDB6954ADDD028C88780C7F91644AE79E28738FC002F04C49B1FDF2EC8C3C899C1087A90336A6E67D2E8551955EEE31
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/4CDB6954ADDD028C88780C7F91644AE79E28738FC002F04C49B1FDF2EC8C3C899C1087A90336A6E67D2E8551955EEE31
http://www.w3.org/2000/01/rdf-schema#comment
"The mannose-6-phosphate-enzyme complex is developed and the key residues involved in the ligand binding are determined. Our results suggest a hydride transfer mechanism of alpha-hydrogen between the C1 and C2 positions."
xsd:string
http://purl.uniprot.org/uniprot/#_A8759DD4AA90C09B55F6306A2801BEA34F0FF1174761AEC6972744C5CB20E7E27ACE52098724E4297E9E265FA890C370
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/4CDB6954ADDD028C88780C7F91644AE79E28738FC002F04C49B1FDF2EC8C3C899C1087A90336A6E67D2E8551955EEE31
http://purl.uniprot.org/uniprot/H3BPP3
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/4CDB6954ADDD028C88780C7F91644AE79E28738FC002F04C49B1FDF2EC8C3C899C1087A90336A6E67D2E8551955EEE31
http://purl.uniprot.org/uniprot/#_H3BPP3-mappedCitation-16488169
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/4CDB6954ADDD028C88780C7F91644AE79E28738FC002F04C49B1FDF2EC8C3C899C1087A90336A6E67D2E8551955EEE31