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1VBT

Structure of cyclophilin complexed with sulfur-substituted tetrapeptide AAPF

Functional Information from GO Data
ChainGOidnamespacecontents
A0000413biological_processprotein peptidyl-prolyl isomerization
A0001933biological_processnegative regulation of protein phosphorylation
A0001934biological_processpositive regulation of protein phosphorylation
A0003723molecular_functionRNA binding
A0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
A0005178molecular_functionintegrin binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005925cellular_componentfocal adhesion
A0006457biological_processprotein folding
A0006469biological_processnegative regulation of protein kinase activity
A0006915biological_processapoptotic process
A0016018molecular_functioncyclosporin A binding
A0016020cellular_componentmembrane
A0019076biological_processviral release from host cell
A0030168biological_processplatelet activation
A0030182biological_processneuron differentiation
A0030593biological_processneutrophil chemotaxis
A0030595biological_processleukocyte chemotaxis
A0031982cellular_componentvesicle
A0032148biological_processactivation of protein kinase B activity
A0032873biological_processnegative regulation of stress-activated MAPK cascade
A0032991cellular_componentprotein-containing complex
A0034389biological_processlipid droplet organization
A0034599biological_processcellular response to oxidative stress
A0034774cellular_componentsecretory granule lumen
A0035307biological_processpositive regulation of protein dephosphorylation
A0042118biological_processendothelial cell activation
A0043410biological_processpositive regulation of MAPK cascade
A0045069biological_processregulation of viral genome replication
A0045070biological_processpositive regulation of viral genome replication
A0046790molecular_functionvirion binding
A0050714biological_processpositive regulation of protein secretion
A0051082molecular_functionunfolded protein binding
A0051092biological_processpositive regulation of NF-kappaB transcription factor activity
A0060352biological_processcell adhesion molecule production
A0061944biological_processnegative regulation of protein K48-linked ubiquitination
A0070062cellular_componentextracellular exosome
A0070527biological_processplatelet aggregation
A1902176biological_processnegative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway
A1903901biological_processnegative regulation of viral life cycle
A1904399molecular_functionheparan sulfate binding
A1904813cellular_componentficolin-1-rich granule lumen
A2001233biological_processregulation of apoptotic signaling pathway
B0000413biological_processprotein peptidyl-prolyl isomerization
B0001933biological_processnegative regulation of protein phosphorylation
B0001934biological_processpositive regulation of protein phosphorylation
B0003723molecular_functionRNA binding
B0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
B0005178molecular_functionintegrin binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005925cellular_componentfocal adhesion
B0006457biological_processprotein folding
B0006469biological_processnegative regulation of protein kinase activity
B0006915biological_processapoptotic process
B0016018molecular_functioncyclosporin A binding
B0016020cellular_componentmembrane
B0019076biological_processviral release from host cell
B0030168biological_processplatelet activation
B0030182biological_processneuron differentiation
B0030593biological_processneutrophil chemotaxis
B0030595biological_processleukocyte chemotaxis
B0031982cellular_componentvesicle
B0032148biological_processactivation of protein kinase B activity
B0032873biological_processnegative regulation of stress-activated MAPK cascade
B0032991cellular_componentprotein-containing complex
B0034389biological_processlipid droplet organization
B0034599biological_processcellular response to oxidative stress
B0034774cellular_componentsecretory granule lumen
B0035307biological_processpositive regulation of protein dephosphorylation
B0042118biological_processendothelial cell activation
B0043410biological_processpositive regulation of MAPK cascade
B0045069biological_processregulation of viral genome replication
B0045070biological_processpositive regulation of viral genome replication
B0046790molecular_functionvirion binding
B0050714biological_processpositive regulation of protein secretion
B0051082molecular_functionunfolded protein binding
B0051092biological_processpositive regulation of NF-kappaB transcription factor activity
B0060352biological_processcell adhesion molecule production
B0061944biological_processnegative regulation of protein K48-linked ubiquitination
B0070062cellular_componentextracellular exosome
B0070527biological_processplatelet aggregation
B1902176biological_processnegative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway
B1903901biological_processnegative regulation of viral life cycle
B1904399molecular_functionheparan sulfate binding
B1904813cellular_componentficolin-1-rich granule lumen
B2001233biological_processregulation of apoptotic signaling pathway
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR CHAIN C OF SULFUR-SUBSTITUTED TETRAPEPTIDE
ChainResidue
AARG55
BTRP121
DPHE4
AILE57
APHE60
AMET61
AASN102
APHE113
ATRP121
ALEU122
AHIS126

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR CHAIN D OF SULFUR-SUBSTITUTED TETRAPEPTIDE
ChainResidue
ATRP121
BARG55
BILE57
BPHE60
BGLN63
BALA101
BASN102
BTRP121
BLEU122
BHIS126
CPHE4

Functional Information from PROSITE/UniProt
site_idPS00170
Number of Residues18
DetailsCSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YkgScFHRIIpgFMcQGG
ChainResidueDetails
ATYR48-GLY65

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712
ChainResidueDetails
BVAL2
AVAL2

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylvaline; partial; in Peptidyl-prolyl cis-trans isomerase A, N-terminally processed => ECO:0000269|PubMed:25489052, ECO:0000269|Ref.12, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:25944712
ChainResidueDetails
AASN3
BASN3

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
AVAL29
APHE83
BVAL29
BPHE83

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
AGLY45
ASER77
AVAL132
BGLY45
BSER77
BVAL132

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
AILE78
BILE78

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:20068231
ChainResidueDetails
AGLY94
BGLY94

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:20364129, ECO:0000269|PubMed:25678563, ECO:0007744|PubMed:19608861
ChainResidueDetails
AHIS126
BHIS126

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P17742
ChainResidueDetails
AGLU134
BGLU134

site_idSWS_FT_FI9
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BGLY109
AGLY109

site_idSWS_FT_FI10
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
ChainResidueDetails
AVAL29
BVAL29

site_idSWS_FT_FI11
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
ChainResidueDetails
APHE83
BPHE83

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 189
ChainResidueDetails
AILE56electrostatic stabiliser, hydrogen bond donor, steric role
AMET61polar/non-polar interaction, steric role
AGLY64electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
AALA103electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
AILE114polar/non-polar interaction, steric role
AASP123polar/non-polar interaction, steric role
AVAL127polar/non-polar interaction, steric role

site_idMCSA2
Number of Residues7
DetailsM-CSA 189
ChainResidueDetails
BILE56electrostatic stabiliser, hydrogen bond donor, steric role
BMET61polar/non-polar interaction, steric role
BGLY64electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
BALA103electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
BILE114polar/non-polar interaction, steric role
BASP123polar/non-polar interaction, steric role
BVAL127polar/non-polar interaction, steric role

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PDB entries from 2024-05-01

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