Structure of PDB 7pcj Chain D Binding Site BS03

Receptor Information
>7pcj Chain D (length=164) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGS
CFHRIIPGFMCQGGDFTRHNGTGGKSIYGEKFEDENFILKHTGPGILSMA
NAGPNTNGSQFFICTAKTEWLDGCHVVFGKVKEGMNIVEAMERFGSRNGK
TSKKITIADCGQLE
Ligand information
Ligand ID7IB
InChIInChI=1S/C14H14N2O4/c15-10-6-4-8(2-1-3-12(17)18)9-5-7-11(14(19)20)16-13(9)10/h4-7H,1-3,15H2,(H,17,18)(H,19,20)
InChIKeyAHGXWTCIRIDJEN-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.385Nc1ccc(CCCC(O)=O)c2ccc(nc12)C(O)=O
OpenEye OEToolkits 2.0.7c1cc(c2c(c1CCCC(=O)O)ccc(n2)C(=O)O)N
FormulaC14 H14 N2 O4
Name8-azanyl-5-(4-oxidanyl-4-oxidanylidene-butyl)quinoline-2-carboxylic acid
ChEMBL
DrugBank
ZINC
PDB chain7pcj Chain D Residue 205 [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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PDB7pcj X-ray structure of a cystein mutant of Cyclophilin A tethered to an aromatic oligoamide foldamer complexed with Cyclosporin A
Resolution1.91 Å
Binding residue
(original residue number in PDB)		K30 K93
Binding residue
(residue number reindexed from 1)		K27 K90
Annotation score1
Enzymatic activity
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
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Biological Process
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Cellular Component
External links
PDB RCSB:7pcj, PDBe:7pcj, PDBj:7pcj
PDBsum7pcj
PubMed
UniProtP62937|PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A (Gene Name=PPIA)

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