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DESCRIBE <http://purl.uniprot.org/SHA-384/22B38282952F46B38BFBDD99E2EA4A3BEBCDA055851B04D765497D9BE819CBBB587AE5A17A39803E4BCBCD56885E8CBE>
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http://purl.uniprot.org/SHA-384/22B38282952F46B38BFBDD99E2EA4A3BEBCDA055851B04D765497D9BE819CBBB587AE5A17A39803E4BCBCD56885E8CBE
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/22B38282952F46B38BFBDD99E2EA4A3BEBCDA055851B04D765497D9BE819CBBB587AE5A17A39803E4BCBCD56885E8CBE
http://www.w3.org/2000/01/rdf-schema#comment
"Results show that both wild-type and mutant proteins bind heme in a 1:1 fashion possessing tight ferric heme affinities and its measured reduction potential was found to be similar to that of other monotyrosinate hemoproteins."
xsd:string
http://purl.uniprot.org/uniprot/#_B8EF417494734B678F36CF12D9CB58BF59387394B8C1C51B756DA2B267691E6AF4D8D4A7924FCC644B1B0E7DE7599CEB
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/22B38282952F46B38BFBDD99E2EA4A3BEBCDA055851B04D765497D9BE819CBBB587AE5A17A39803E4BCBCD56885E8CBE
http://purl.uniprot.org/uniprot/Q12091
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/22B38282952F46B38BFBDD99E2EA4A3BEBCDA055851B04D765497D9BE819CBBB587AE5A17A39803E4BCBCD56885E8CBE
http://purl.uniprot.org/uniprot/#_Q12091-mappedCitation-18031064
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/22B38282952F46B38BFBDD99E2EA4A3BEBCDA055851B04D765497D9BE819CBBB587AE5A17A39803E4BCBCD56885E8CBE