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2X2D

acetyl-CypA:HIV-1 N-term capsid domain complex

Functional Information from GO Data
ChainGOidnamespacecontents
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
B0016853molecular_functionisomerase activity
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
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
C0000413biological_processprotein peptidyl-prolyl isomerization
C0001933biological_processnegative regulation of protein phosphorylation
C0001934biological_processpositive regulation of protein phosphorylation
C0003723molecular_functionRNA binding
C0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
C0005178molecular_functionintegrin binding
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005925cellular_componentfocal adhesion
C0006457biological_processprotein folding
C0006469biological_processnegative regulation of protein kinase activity
C0006915biological_processapoptotic process
C0016018molecular_functioncyclosporin A binding
C0016020cellular_componentmembrane
C0016853molecular_functionisomerase activity
C0019076biological_processviral release from host cell
C0030168biological_processplatelet activation
C0030182biological_processneuron differentiation
C0030593biological_processneutrophil chemotaxis
C0030595biological_processleukocyte chemotaxis
C0031982cellular_componentvesicle
C0032148biological_processactivation of protein kinase B activity
C0032873biological_processnegative regulation of stress-activated MAPK cascade
C0032991cellular_componentprotein-containing complex
C0034389biological_processlipid droplet organization
C0034599biological_processcellular response to oxidative stress
C0034774cellular_componentsecretory granule lumen
C0042118biological_processendothelial cell activation
C0043410biological_processpositive regulation of MAPK cascade
C0045069biological_processregulation of viral genome replication
C0045070biological_processpositive regulation of viral genome replication
C0046790molecular_functionvirion binding
C0050714biological_processpositive regulation of protein secretion
C0051082molecular_functionunfolded protein binding
C0051092biological_processpositive regulation of NF-kappaB transcription factor activity
C0060352biological_processcell adhesion molecule production
C0061944biological_processnegative regulation of protein K48-linked ubiquitination
C0070062cellular_componentextracellular exosome
C0070527biological_processplatelet aggregation
C1902176biological_processnegative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway
C1903901biological_processnegative regulation of viral life cycle
C1904399molecular_functionheparan sulfate binding
C1904813cellular_componentficolin-1-rich granule lumen
C2001233biological_processregulation of apoptotic signaling pathway
D0016032biological_processviral process
E0016032biological_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
BTYR48-GLY65

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsModified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25944712","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"N-acetylvaline; partial; in Peptidyl-prolyl cis-trans isomerase A, N-terminally processed","evidences":[{"source":"PubMed","id":"25489052","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2005","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Claeys D."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25944712","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"20364129","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25678563","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P17742","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues76
DetailsRegion: {"description":"Interaction with human PPIA/CYPA and NUP153","evidences":[{"source":"PubMed","id":"19369352","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24130490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8980234","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues16
DetailsRegion: {"description":"PPIA/CYPA-binding loop","evidences":[{"source":"UniProtKB","id":"P04591","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by host MAPK1","evidences":[{"source":"PubMed","id":"24509437","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues2
DetailsSite: {"description":"Cis/trans isomerization of proline peptide bond; by human PPIA/CYPA","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 189
ChainResidueDetails

site_idMCSA2
Number of Residues7
DetailsM-CSA 189
ChainResidueDetails
BARG55electrostatic stabiliser, hydrogen bond donor, steric role
BPHE60polar/non-polar interaction, steric role
BGLN63electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
BASN102electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
BPHE113polar/non-polar interaction, steric role
BLEU122polar/non-polar interaction, steric role
BGLY130polar/non-polar interaction, steric role

239803

PDB entries from 2025-08-06

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