Structure of PDB 6x4n Chain A Binding Site BS01

Receptor Information
>6x4n Chain A (length=165) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
HMVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYK
GSCFHRIIPGFMCQGGDFTRHNGTGGKSIYGEKFEDENFILKHTGPGILS
MANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRN
GKTSKKITIADCGQL
Ligand information
Ligand IDUOD
InChIInChI=1S/C30H39N5O5/c1-17(2)25-26(36)31-18(3)27(37)35-15-7-8-23(34-35)28(38)40-19(4)22-12-11-21-10-9-20(16-24(21)32-22)13-14-30(5,6)29(39)33-25/h9-14,16-19,23,25,34H,7-8,15H2,1-6H3,(H,31,36)(H,33,39)/b14-13+/t18-,19+,23-,25-/m0/s1
InChIKeyXCZDYKRNHKYRTQ-HQHUNAKVSA-N
SMILES
SoftwareSMILES
CACTVS 3.385CC(C)[CH]1NC(=O)C(C)(C)C=Cc2ccc3ccc(nc3c2)[CH](C)OC(=O)[CH]4CCC[N](N4)C(=O)[CH](C)NC1=O
CACTVS 3.385CC(C)[C@@H]1NC(=O)C(C)(C)\C=C\c2ccc3ccc(nc3c2)[C@@H](C)OC(=O)[C@@H]4CCC[N@@](N4)C(=O)[C@H](C)NC1=O
OpenEye OEToolkits 2.0.7C[C@@H]1c2ccc3ccc(cc3n2)/C=C/C(C(=O)N[C@H](C(=O)N[C@H](C(=O)N4CCC[C@H](N4)C(=O)O1)C)C(C)C)(C)C
ACDLabs 12.01c1cc2nc4c1ccc(C=CC(C(=O)NC(C(NC(C(N3CCCC(C(OC2C)=O)N3)=O)C)=O)C(C)C)(C)C)c4
OpenEye OEToolkits 2.0.7CC1c2ccc3ccc(cc3n2)C=CC(C(=O)NC(C(=O)NC(C(=O)N4CCCC(N4)C(=O)O1)C)C(C)C)(C)C
FormulaC30 H39 N5 O5
Name(2R,5S,11S,14S,18E)-2,11,17,17-tetramethyl-14-(propan-2-yl)-3-oxa-9,12,15,26,29-pentaazatetracyclo[18.5.3.1~5,9~.0~23,27~]nonacosa-1(25),18,20(28),21,23,26-hexaene-4,10,13,16-tetrone
ChEMBLCHEMBL4168950
DrugBank
ZINC
PDB chain6x4n Chain A Residue 400 [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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PDB6x4n Evaluation of Free Energy Calculations for the Prioritization of Macrocycle Synthesis.
Resolution1.51 Å
Binding residue
(original residue number in PDB)		R55 Q63 G72 A101 N102 Q111 F113
Binding residue
(residue number reindexed from 1)		R56 Q64 G73 A102 N103 Q112 F114
Annotation score1
Binding affinityMOAD: Kd=4nM
BindingDB: Kd=4.0nM
Enzymatic activity
Catalytic site (original residue number in PDB) R55 F60 Q63 N102 F113 L122 H126
Catalytic site (residue number reindexed from 1) R56 F61 Q64 N103 F114 L123 H127
Enzyme Commision number 5.2.1.8: peptidylprolyl isomerase.
Gene Ontology
Molecular Function
GO:0003723 RNA binding
GO:0003755 peptidyl-prolyl cis-trans isomerase activity
GO:0005178 integrin binding
GO:0005515 protein binding
GO:0016018 cyclosporin A binding
GO:0046790 virion binding
GO:0051082 unfolded protein binding
GO:1904399 heparan sulfate binding
Biological Process
GO:0000413 protein peptidyl-prolyl isomerization
GO:0001933 negative regulation of protein phosphorylation
GO:0001934 positive regulation of protein phosphorylation
GO:0006457 protein folding
GO:0006469 negative regulation of protein kinase activity
GO:0006915 apoptotic process
GO:0019076 viral release from host cell
GO:0030168 platelet activation
GO:0030182 neuron differentiation
GO:0030593 neutrophil chemotaxis
GO:0030595 leukocyte chemotaxis
GO:0032148 activation of protein kinase B activity
GO:0032873 negative regulation of stress-activated MAPK cascade
GO:0034389 lipid droplet organization
GO:0034599 cellular response to oxidative stress
GO:0042118 endothelial cell activation
GO:0043410 positive regulation of MAPK cascade
GO:0045069 regulation of viral genome replication
GO:0045070 positive regulation of viral genome replication
GO:0050714 positive regulation of protein secretion
GO:0051092 positive regulation of NF-kappaB transcription factor activity
GO:0060352 cell adhesion molecule production
GO:0061944 negative regulation of protein K48-linked ubiquitination
GO:0070527 platelet aggregation
GO:1902176 negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway
GO:1903901 negative regulation of viral life cycle
GO:2001233 regulation of apoptotic signaling pathway
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005925 focal adhesion
GO:0016020 membrane
GO:0031982 vesicle
GO:0032991 protein-containing complex
GO:0034774 secretory granule lumen
GO:0070062 extracellular exosome
GO:1904813 ficolin-1-rich granule lumen

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Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:6x4n, PDBe:6x4n, PDBj:6x4n
PDBsum6x4n
PubMed32539379
UniProtP62937|PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A (Gene Name=PPIA)

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