Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6Y9Y

Structure of the native full-length HIV-1 capsid protein in complex with Cyclophilin A from helical assembly (-7,13)

Functional Information from GO Data
ChainGOidnamespacecontents
A0016032biological_processviral process
B0016032biological_processviral process
C0016032biological_processviral process
d0016032biological_processviral process
D0016032biological_processviral process
e0016032biological_processviral process
G0016032biological_processviral process
H0016032biological_processviral process
j0016032biological_processviral process
J0000413biological_processprotein peptidyl-prolyl isomerization
J0001933biological_processnegative regulation of protein phosphorylation
J0001934biological_processpositive regulation of protein phosphorylation
J0003723molecular_functionRNA binding
J0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
J0005178molecular_functionintegrin binding
J0005515molecular_functionprotein binding
J0005576cellular_componentextracellular region
J0005615cellular_componentextracellular space
J0005634cellular_componentnucleus
J0005737cellular_componentcytoplasm
J0005829cellular_componentcytosol
J0005925cellular_componentfocal adhesion
J0006457biological_processprotein folding
J0006469biological_processnegative regulation of protein kinase activity
J0006915biological_processapoptotic process
J0016018molecular_functioncyclosporin A binding
J0016020cellular_componentmembrane
J0019076biological_processviral release from host cell
J0030168biological_processplatelet activation
J0030182biological_processneuron differentiation
J0030593biological_processneutrophil chemotaxis
J0030595biological_processleukocyte chemotaxis
J0031982cellular_componentvesicle
J0032148biological_processactivation of protein kinase B activity
J0032873biological_processnegative regulation of stress-activated MAPK cascade
J0032991cellular_componentprotein-containing complex
J0034389biological_processlipid droplet organization
J0034599biological_processcellular response to oxidative stress
J0034774cellular_componentsecretory granule lumen
J0035307biological_processpositive regulation of protein dephosphorylation
J0042118biological_processendothelial cell activation
J0043410biological_processpositive regulation of MAPK cascade
J0045069biological_processregulation of viral genome replication
J0045070biological_processpositive regulation of viral genome replication
J0046790molecular_functionvirion binding
J0050714biological_processpositive regulation of protein secretion
J0051082molecular_functionunfolded protein binding
J0051092biological_processpositive regulation of NF-kappaB transcription factor activity
J0060352biological_processcell adhesion molecule production
J0061944biological_processnegative regulation of protein K48-linked ubiquitination
J0070062cellular_componentextracellular exosome
J0070527biological_processplatelet aggregation
J1902176biological_processnegative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway
J1903901biological_processnegative regulation of viral life cycle
J1904399molecular_functionheparan sulfate binding
J1904813cellular_componentficolin-1-rich granule lumen
J2001233biological_processregulation of apoptotic signaling pathway
k0016032biological_processviral process
N0016032biological_processviral process
Y0016032biological_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
JTYR48-GLY65

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
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
JVAL2
eGLY89
jGLY89
kGLY89
BGLY89
CGLY89
DGLY89
GGLY89
HGLY89
NGLY89
YGLY89
dGLY89

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
JLYS28
eSER16
jSER16
kSER16
JLYS82
CSER16
DSER16
GSER16
HSER16
NSER16
YSER16
dSER16

site_idSWS_FT_FI3
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
JLYS44
JLYS76
JLYS131

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
JSER77

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:20068231
ChainResidueDetails
JTHR93

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:20364129, ECO:0000269|PubMed:25678563, ECO:0007744|PubMed:19608861
ChainResidueDetails
JLYS125

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P17742
ChainResidueDetails
JLYS133

site_idSWS_FT_FI8
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
JASN108

site_idSWS_FT_FI9
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
ChainResidueDetails
JLYS28

site_idSWS_FT_FI10
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
ChainResidueDetails
JLYS82

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 189
ChainResidueDetails
JARG55electrostatic stabiliser, hydrogen bond donor, steric role
JPHE60polar/non-polar interaction, steric role
JGLN63electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
JASN102electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
JPHE113polar/non-polar interaction, steric role
JLEU122polar/non-polar interaction, steric role
JHIS126polar/non-polar interaction, steric role

219140

PDB entries from 2024-05-01

PDB statisticsPDBj update infoContact PDBjnumon