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4DGE

TRIMCyp cyclophilin domain from Macaca mulatta: H70C mutant, HIV-1 CA(O-loop) complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000413biological_processprotein peptidyl-prolyl isomerization
A0001933biological_processnegative regulation of protein phosphorylation
A0001934biological_processpositive regulation of protein phosphorylation
A0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
A0005178molecular_functionintegrin binding
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006457biological_processprotein folding
A0006469biological_processnegative regulation of protein kinase activity
A0006915biological_processapoptotic process
A0016018molecular_functioncyclosporin A binding
A0030168biological_processplatelet activation
A0030593biological_processneutrophil chemotaxis
A0030595biological_processleukocyte chemotaxis
A0032148biological_processactivation of protein kinase B activity
A0032873biological_processnegative regulation of stress-activated MAPK cascade
A0034599biological_processcellular response to oxidative stress
A0035307biological_processpositive regulation of protein dephosphorylation
A0042118biological_processendothelial cell activation
A0043410biological_processpositive regulation of MAPK cascade
A0045069biological_processregulation of viral genome replication
A0051092biological_processpositive regulation of NF-kappaB transcription factor activity
A0060352biological_processcell adhesion molecule production
A0061944biological_processnegative regulation of protein K48-linked ubiquitination
A0070527biological_processplatelet aggregation
A1902176biological_processnegative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway
A1904399molecular_functionheparan sulfate binding
A2001233biological_processregulation of apoptotic signaling pathway
B0000413biological_processprotein peptidyl-prolyl isomerization
B0001933biological_processnegative regulation of protein phosphorylation
B0001934biological_processpositive regulation of protein phosphorylation
B0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
B0005178molecular_functionintegrin binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006457biological_processprotein folding
B0006469biological_processnegative regulation of protein kinase activity
B0006915biological_processapoptotic process
B0016018molecular_functioncyclosporin A binding
B0030168biological_processplatelet activation
B0030593biological_processneutrophil chemotaxis
B0030595biological_processleukocyte chemotaxis
B0032148biological_processactivation of protein kinase B activity
B0032873biological_processnegative regulation of stress-activated MAPK cascade
B0034599biological_processcellular response to oxidative stress
B0035307biological_processpositive regulation of protein dephosphorylation
B0042118biological_processendothelial cell activation
B0043410biological_processpositive regulation of MAPK cascade
B0045069biological_processregulation of viral genome replication
B0051092biological_processpositive regulation of NF-kappaB transcription factor activity
B0060352biological_processcell adhesion molecule production
B0061944biological_processnegative regulation of protein K48-linked ubiquitination
B0070527biological_processplatelet aggregation
B1902176biological_processnegative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway
B1904399molecular_functionheparan sulfate binding
B2001233biological_processregulation of apoptotic signaling pathway
C0016032biological_processviral process
D0016032biological_processviral process
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
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
CMET0
DMET0

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cis/trans isomerization of proline peptide bond; by human PPIA/CYPA => ECO:0000250
ChainResidueDetails
CGLY89
DGLY89

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by host => ECO:0000250
ChainResidueDetails
CMET0
DMET0
BLYS28
BLYS82

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine; by host MAPK1 => ECO:0000269|PubMed:24509437
ChainResidueDetails
CSER16
DSER16
ALYS125
ALYS131
BLYS44
BLYS76
BLYS125
BLYS131

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P62937
ChainResidueDetails
ASER77
BSER77

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P62937
ChainResidueDetails
ATHR93
BTHR93

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P17742
ChainResidueDetails
ALYS133
BLYS133

site_idSWS_FT_FI8
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN108
BASN108

site_idSWS_FT_FI9
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62937
ChainResidueDetails
ALYS28
BLYS28

site_idSWS_FT_FI10
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P62937
ChainResidueDetails
ALYS82
BLYS82

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PDB entries from 2024-06-05

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