Structure of PDB 8pdf Chain A Binding Site BS01

Receptor Information
>8pdf Chain A (length=107) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GVQVETISPGDGRTFPKRGQTVVVHYTGMLEDGKKFDSSRDRNKPFKFML
GKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGATGHPGIIPPHATLVFD
VELLKLE
Ligand information
Ligand IDY5Q
InChIInChI=1S/C48H61Cl2N9O9S2/c1-7-32-24-57(46(63)40-10-8-9-39(32)59(40)70(65,66)37-20-34(49)19-35(50)21-37)30(3)38-26-56(55-54-38)15-16-67-17-18-68-27-42(61)53-44(48(4,5)6)47(64)58-25-36(60)22-41(58)45(62)51-23-31-11-13-33(14-12-31)43-29(2)52-28-69-43/h7,11-14,19-21,26,28,30,32,36,39-41,44,60H,1,8-10,15-18,22-25,27H2,2-6H3,(H,51,62)(H,53,61)/t30-,32-,36+,39+,40-,41-,44+/m0/s1
InChIKeyMFMLZZDFONRVIU-SNTVEAOZSA-N
SMILES
SoftwareSMILES
CACTVS 3.385C[CH](N1C[CH](C=C)[CH]2CCC[CH](N2[S](=O)(=O)c3cc(Cl)cc(Cl)c3)C1=O)c4cn(CCOCCOCC(=O)N[CH](C(=O)N5C[CH](O)C[CH]5C(=O)NCc6ccc(cc6)c7scnc7C)C(C)(C)C)nn4
OpenEye OEToolkits 2.0.7Cc1c(scn1)c2ccc(cc2)CNC(=O)[C@@H]3C[C@H](CN3C(=O)[C@H](C(C)(C)C)NC(=O)COCCOCCn4cc(nn4)[C@H](C)N5C[C@@H]([C@H]6CCC[C@@H](C5=O)N6S(=O)(=O)c7cc(cc(c7)Cl)Cl)C=C)O
CACTVS 3.385C[C@H](N1C[C@H](C=C)[C@H]2CCC[C@H](N2[S](=O)(=O)c3cc(Cl)cc(Cl)c3)C1=O)c4cn(CCOCCOCC(=O)N[C@H](C(=O)N5C[C@H](O)C[C@H]5C(=O)NCc6ccc(cc6)c7scnc7C)C(C)(C)C)nn4
OpenEye OEToolkits 2.0.7Cc1c(scn1)c2ccc(cc2)CNC(=O)C3CC(CN3C(=O)C(C(C)(C)C)NC(=O)COCCOCCn4cc(nn4)C(C)N5CC(C6CCCC(C5=O)N6S(=O)(=O)c7cc(cc(c7)Cl)Cl)C=C)O
FormulaC48 H61 Cl2 N9 O9 S2
Name(2~{S},4~{R})-1-[(2~{S})-2-[2-[2-[2-[4-[(1~{S})-1-[(1~{S},5~{S},6~{R})-10-[3,5-bis(chloranyl)phenyl]sulfonyl-5-ethenyl-2-oxidanylidene-3,10-diazabicyclo[4.3.1]decan-3-yl]ethyl]-1,2,3-triazol-1-yl]ethoxy]ethoxy]ethanoylamino]-3,3-dimethyl-butanoyl]-~{N}-[[4-(4-methyl-1,3-thiazol-5-yl)phenyl]methyl]-4-oxidanyl-pyrrolidine-2-carboxamide
ChEMBL
DrugBank
ZINC
PDB chain8pdf Chain A Residue 201 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB8pdf Discovery of a Potent PROTAC Enables Targeting of FKBP51's Scaffolding Functions.
Resolution1.2 Å
Binding residue
(original residue number in PDB)		Y26 F36 D37 F46 E54 V55 I56 W59 Y82 H87 F99
Binding residue
(residue number reindexed from 1)		Y26 F36 D37 F46 E54 V55 I56 W59 Y82 H87 F99
Annotation score1
Enzymatic activity
Enzyme Commision number 5.2.1.8: peptidylprolyl isomerase.
Gene Ontology
Molecular Function
GO:0003755 peptidyl-prolyl cis-trans isomerase activity
GO:0005160 transforming growth factor beta receptor binding
GO:0005515 protein binding
GO:0005527 macrolide binding
GO:0005528 FK506 binding
GO:0016247 channel regulator activity
GO:0030547 signaling receptor inhibitor activity
GO:0034713 type I transforming growth factor beta receptor binding
GO:0044325 transmembrane transporter binding
GO:0070411 I-SMAD binding
GO:0070697 activin receptor binding
Biological Process
GO:0000413 protein peptidyl-prolyl isomerization
GO:0003007 heart morphogenesis
GO:0006457 protein folding
GO:0006458 'de novo' protein folding
GO:0014809 regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion
GO:0022417 protein maturation by protein folding
GO:0030512 negative regulation of transforming growth factor beta receptor signaling pathway
GO:0032092 positive regulation of protein binding
GO:0032880 regulation of protein localization
GO:0032926 negative regulation of activin receptor signaling pathway
GO:0042026 protein refolding
GO:0042110 T cell activation
GO:0043123 positive regulation of canonical NF-kappaB signal transduction
GO:0050776 regulation of immune response
GO:0055010 ventricular cardiac muscle tissue morphogenesis
GO:0060314 regulation of ryanodine-sensitive calcium-release channel activity
GO:0060347 heart trabecula formation
GO:0070588 calcium ion transmembrane transport
GO:0097435 supramolecular fiber organization
GO:1902991 regulation of amyloid precursor protein catabolic process
GO:1990000 amyloid fibril formation
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0014802 terminal cisterna
GO:0016020 membrane
GO:0016529 sarcoplasmic reticulum
GO:0030018 Z disc
GO:0033017 sarcoplasmic reticulum membrane
GO:0098562 cytoplasmic side of membrane
GO:1990425 ryanodine receptor complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:8pdf, PDBe:8pdf, PDBj:8pdf
PDBsum8pdf
PubMed37942685
UniProtP62942|FKB1A_HUMAN Peptidyl-prolyl cis-trans isomerase FKBP1A (Gene Name=FKBP1A)

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