Structure of PDB 3fap Chain A Binding Site BS01

Receptor Information
>3fap 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]
GVQVETISPGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFML
GKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGATGHPGIIPPHATLVFD
VELLKLE
Ligand information
Ligand IDARD
InChIInChI=1S/C55H81NO12S/c1-32-16-12-11-13-17-33(2)42(48-24-20-39(8)69-48)30-41-22-19-38(7)55(64,68-41)52(61)53(62)56-25-15-14-18-43(56)54(63)67-46(35(4)28-40-21-23-44(57)47(29-40)65-9)31-45(58)34(3)27-37(6)50(60)51(66-10)49(59)36(5)26-32/h11-13,16-17,20,24,27,32,34-36,38,40-44,46-47,50-51,57,60,64H,14-15,18-19,21-23,25-26,28-31H2,1-10H3/b13-11+,16-12+,33-17+,37-27+/t32-,34-,35-,36-,38-,40+,41+,42-,43+,44-,46+,47-,50-,51+,55-/m1/s1
InChIKeySDSGJAIFUCCAOV-MSLSVLDMSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0Cc1ccc(s1)[C@@H]/2C[C@@H]3CC[C@H]([C@@](O3)(C(=O)C(=O)N4CCCC[C@H]4C(=O)O[C@@H](CC(=O)[C@@H](\C=C(\[C@H]([C@H](C(=O)[C@@H](C[C@@H](\C=C\C=C\C=C2/C)C)C)OC)O)/C)C)[C@H](C)C[C@@H]5CC[C@H]([C@@H](C5)OC)O)O)C
ACDLabs 10.04O=C2C(=O)C5(OC(CC(c1sc(cc1)C)C(=CC=CC=CC(C)CC(C(=O)C(OC)C(O)C(=CC(C(=O)CC(OC(=O)C3N2CCCC3)C(C)CC4CCC(O)C(OC)C4)C)C)C)C)CCC5C)O
CACTVS 3.341CO[CH]1C[CH](CC[CH]1O)C[CH](C)[CH]2CC(=O)[CH](C)C=C(C)[CH](O)[CH](OC)C(=O)[CH](C)C[CH](C)C=CC=CC=C(C)[CH](C[CH]3CC[CH](C)[C](O)(O3)C(=O)C(=O)N4CCCC[CH]4C(=O)O2)c5sc(C)cc5
OpenEye OEToolkits 1.5.0Cc1ccc(s1)C2CC3CCC(C(O3)(C(=O)C(=O)N4CCCCC4C(=O)OC(CC(=O)C(C=C(C(C(C(=O)C(CC(C=CC=CC=C2C)C)C)OC)O)C)C)C(C)CC5CCC(C(C5)OC)O)O)C
CACTVS 3.341CO[C@@H]1C[C@@H](CC[C@H]1O)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=C/C=C(C)/[C@@H](C[C@@H]3CC[C@@H](C)[C@@](O)(O3)C(=O)C(=O)N4CCCC[C@H]4C(=O)O2)c5sc(C)cc5
FormulaC55 H81 N O12 S
NameC15-(R)-METHYLTHIENYL RAPAMYCIN;
RAPAMYCIN IMMUNOSUPPRESSANT DRUG
ChEMBLCHEMBL263850
DrugBank
ZINCZINC000263621026
PDB chain3fap Chain A Residue 402 [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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PDB3fap Refined structure of the FKBP12-rapamycin-FRB ternary complex at 2.2 A resolution.
Resolution1.85 Å
Binding residue
(original residue number in PDB)		Y26 F36 D37 R42 F46 Q53 E54 V55 I56 W59 Y82 I91
Binding residue
(residue number reindexed from 1)		Y26 F36 D37 R42 F46 Q53 E54 V55 I56 W59 Y82 I91
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) Y26 F36 D37 I56 Y82 F99
Catalytic site (residue number reindexed from 1) Y26 F36 D37 I56 Y82 F99
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:3fap, PDBe:3fap, PDBj:3fap
PDBsum3fap
PubMed10089303
UniProtP62942|FKB1A_HUMAN Peptidyl-prolyl cis-trans isomerase FKBP1A (Gene Name=FKBP1A)

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