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2XGY

Complex of Rabbit Endogenous Lentivirus (RELIK)Capsid with Cyclophilin A

Functional Information from GO Data
ChainGOidnamespacecontents
A0016032biological_processviral process
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
B0005886cellular_componentplasma membrane
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
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
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 1138
ChainResidue
AASN53
AASN57
AILE70
AILE73
AARG103
ATYR124
AHOH2136

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 1166
ChainResidue
AHOH2100
BGLY59
BPHE60
BTRP121
BHOH2229
BHOH2230
AHIS84
AASP90

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 Residues156
DetailsDomain: {"description":"PPIase cyclophilin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00156","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
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_FI3
Number of Residues1
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_FI4
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
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_FI9
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P17742","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate"}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
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
BHIS126polar/non-polar interaction, steric role

247536

PDB entries from 2026-01-14

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