Structure of PDB 1awv Chain F

Receptor sequence
>1awvF (length=164) Species: 9606 (Homo sapiens) [Search protein sequence]
VNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGS
CFHRIIPGFMCQGGDFTRHNGTGGKSIYGEKFEDENFILKHTGPGILSMA
NAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGK
TSKKITIADCGQLE
3D structure
PDB1awv Crystal structure of cyclophilin A complexed with a binding site peptide from the HIV-1 capsid protein.
ChainF
Resolution2.34 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R1055 F1060 Q1063 N1102 F1113 L1122 H1126
Catalytic site (residue number reindexed from 1) R54 F59 Q62 N101 F112 L121 H125
Enzyme Commision number 5.2.1.8: peptidylprolyl isomerase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 peptide F R1055 F1060 Q1063 G1072 T1073 A1103 Q1111 F1113 W1121 H1126 R54 F59 Q62 G71 T72 A102 Q110 F112 W120 H125
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:1awv, PDBe:1awv, PDBj:1awv
PDBsum1awv
PubMed9385632
UniProtP62937|PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A (Gene Name=PPIA)

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