| Reaction Details |
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 | Report a problem with these data |
| Target | Heat shock cognate 71 kDa protein |
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| Ligand | BDBM14487 |
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| Substrate/Competitor | n/a |
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| Meas. Tech. | ChEMBL_1588265 (CHEMBL3825930) |
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| Kd | 112202±n/a nM |
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| Citation |  Cheeseman, MD; Westwood, IM; Barbeau, O; Rowlands, M; Dobson, S; Jones, AM; Jeganathan, F; Burke, R; Kadi, N; Workman, P; Collins, I; van Montfort, RL; Jones, K Exploiting Protein Conformational Change to Optimize Adenosine-Derived Inhibitors of HSP70. J Med Chem59:4625-36 (2016) [PubMed] Article |
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| More Info.: | Get all data from this article, Assay Method |
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| Heat shock cognate 71 kDa protein |
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| Name: | Heat shock cognate 71 kDa protein |
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| Synonyms: | HSC70 | HSP73 | HSP7C_HUMAN | HSPA10 | HSPA8 | heat shock 70kDa protein 8 isoform 1 | heat shock 70kDa protein 8 isoform 2 |
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| Type: | Enzyme Catalytic Domain |
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| Mol. Mass.: | 70887.67 |
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| Organism: | Homo sapiens (Human) |
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| Description: | gi_5729877 |
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| Residue: | 646 |
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| Sequence: | MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVA
MNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPKVQVEYKGETKSFYPEEVS
SMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAA
IAYGLDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNH
FIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRA
RFEELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELN
KSINPDEAVAYGAAVQAAILSGDKSENVQDLLLLDVTPLSLGIETAGGVMTVLIKRNTTI
PTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDI
DANGILNVSAVDKSTGKENKITITNDKGRLSKEDIERMVQEAEKYKAEDEKQRDKVSSKN
SLESYAFNMKATVEDEKLQGKINDEDKQKILDKCNEIINWLDKNQTAEKEEFEHQQKELE
KVCNPIITKLYQSAGGMPGGMPGGFPGGGAPPSGGASSGPTIEEVD
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| BDBM14487 |
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| n/a |
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| Name | BDBM14487 |
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| Synonyms: | (2R,3R,4S,5R)-2-(6-amino-9H-purin-9-yl)-5-(hydroxymethyl)oxolane-3,4-diol | Adenine-beta-D-arabinofuranoside | Adenosine | CHEMBL477 | N6-Methylado | [U-14C]adenosine | cid_191 | cid_60961 |
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| Type | Nucleoside or nucleotide |
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| Emp. Form. | C10H13N5O4 |
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| Mol. Mass. | 267.2413 |
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| SMILES | Nc1ncnc2n(cnc12)[C@@H]1O[C@H](CO)[C@@H](O)[C@H]1O |
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| Structure | 
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