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TargetPeptidyl-prolyl cis-trans isomerase FKBP1A
LigandBDBM36624
Substrate/Competitorn/a
Meas. Tech.FKBP12 Assay
Ki 29±0.0 nM
EC50 300±0.0 nM
Citation Luengo, JIYamashita, DSDunnington, DBeck, AKRozamus, LWYen, HKBossard, MJLevy, MAHand, ANewman-Tarr, T Structure-activity studies of rapamycin analogs: evidence that the C-7 methoxy group is part of the effector domain and positioned at the FKBP12-FRAP interface. Chem Biol2:471-81 (1995) [PubMed]  Article
More Info.:Get all data from this article,  Assay Method
 
Peptidyl-prolyl cis-trans isomerase FKBP1A
Name:Peptidyl-prolyl cis-trans isomerase FKBP1A
Synonyms:12 kDa FK506-binding protein | 12 kDa FKBP | FK506-binding protein 1A | FK506-binding protein 1A (FKBP12) | FKB1A_HUMAN | FKBP-12 | FKBP-1A | FKBP1 | FKBP12 | FKBP1A | Immunophilin FKBP12 | PPIase | PPIase FKBP1A | Peptidyl-prolyl cis-trans isomerase (FKBP) | Rotamase | RyR1/FKBP12 | mTOR/FKBP12A/FKBP12B
Type:Isomerase
Mol. Mass.:11953.09
Organism:Homo sapiens (Human)
Description:P62942
Residue:108
Sequence:
MGVQVETISPGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGW
EEGVAQMSVGQRAKLTISPDYAYGATGHPGIIPPHATLVFDVELLKLE
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  Blast E-value cutoff:
BDBM36624
n/a
NameBDBM36624
Synonyms:Rapamycin C-7, analog 13
TypeSmall organic molecule
Emp. Form.C50H75NO13
Mol. Mass.898.1294
SMILESCO[C@@H]1C[C@H](C[C@@H](C)[C@@H]2CC(=O)[C@H](C)\C=C(C)\[C@@H](O)[C@@H](OC)C(=O)[C@H](C)C[C@H](C)\C=C\C=CC=C(C)C(=O)C[C@@H]3CC[C@@H](C)[C@@](O)(O3)C(=O)C(=O)N3CCCC[C@H]3C(=O)O2)CC[C@H]1O |w:31.30,33.32,c:14,t:29|
Structure
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