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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

4XR8

Crystal structure of the HPV16 E6/E6AP/p53 ternary complex at 2.25 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0006974biological_processDNA damage response
A0008643biological_processcarbohydrate transport
A0015144molecular_functioncarbohydrate transmembrane transporter activity
A0015768biological_processmaltose transport
A0016020cellular_componentmembrane
A0030288cellular_componentouter membrane-bounded periplasmic space
A0034219biological_processcarbohydrate transmembrane transport
A0034289biological_processdetection of maltose stimulus
A0042597cellular_componentperiplasmic space
A0042956biological_processmaltodextrin transmembrane transport
A0043190cellular_componentATP-binding cassette (ABC) transporter complex
A0055052cellular_componentATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing
A0055085biological_processtransmembrane transport
A0060326biological_processcell chemotaxis
A1901982molecular_functionmaltose binding
A1990060cellular_componentmaltose transport complex
B0005515molecular_functionprotein binding
B0006974biological_processDNA damage response
B0008643biological_processcarbohydrate transport
B0015144molecular_functioncarbohydrate transmembrane transporter activity
B0015768biological_processmaltose transport
B0016020cellular_componentmembrane
B0030288cellular_componentouter membrane-bounded periplasmic space
B0034219biological_processcarbohydrate transmembrane transport
B0034289biological_processdetection of maltose stimulus
B0042597cellular_componentperiplasmic space
B0042956biological_processmaltodextrin transmembrane transport
B0043190cellular_componentATP-binding cassette (ABC) transporter complex
B0055052cellular_componentATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing
B0055085biological_processtransmembrane transport
B0060326biological_processcell chemotaxis
B1901982molecular_functionmaltose binding
B1990060cellular_componentmaltose transport complex
C0000976molecular_functiontranscription cis-regulatory region binding
C0003677molecular_functionDNA binding
C0003700molecular_functionDNA-binding transcription factor activity
C0005634cellular_componentnucleus
C0006355biological_processregulation of DNA-templated transcription
C0006915biological_processapoptotic process
D0000976molecular_functiontranscription cis-regulatory region binding
D0003677molecular_functionDNA binding
D0003700molecular_functionDNA-binding transcription factor activity
D0005634cellular_componentnucleus
D0006355biological_processregulation of DNA-templated transcription
D0006915biological_processapoptotic process
F0003677molecular_functionDNA binding
F0005515molecular_functionprotein binding
F0006351biological_processDNA-templated transcription
F0006355biological_processregulation of DNA-templated transcription
F0008270molecular_functionzinc ion binding
F0030162biological_processregulation of proteolysis
F0030165molecular_functionPDZ domain binding
F0030430cellular_componenthost cell cytoplasm
F0032489biological_processregulation of Cdc42 protein signal transduction
F0033668biological_processsymbiont-mediated suppression of host apoptosis
F0039502biological_processsymbiont-mediated suppression of host type I interferon-mediated signaling pathway
F0039548biological_processsymbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity
F0039648biological_processsymbiont-mediated perturbation of host ubiquitin-like protein modification
F0039653biological_processsymbiont-mediated suppression of host transcription
F0042025cellular_componenthost cell nucleus
F0042802molecular_functionidentical protein binding
F0045944biological_processpositive regulation of transcription by RNA polymerase II
F0046872molecular_functionmetal ion binding
F0052150biological_processsymbiont-mediated perturbation of host apoptosis
F0052170biological_processsymbiont-mediated suppression of host innate immune response
F0060255biological_processregulation of macromolecule metabolic process
F0080090biological_processregulation of primary metabolic process
H0003677molecular_functionDNA binding
H0005515molecular_functionprotein binding
H0006351biological_processDNA-templated transcription
H0006355biological_processregulation of DNA-templated transcription
H0008270molecular_functionzinc ion binding
H0030162biological_processregulation of proteolysis
H0030165molecular_functionPDZ domain binding
H0030430cellular_componenthost cell cytoplasm
H0032489biological_processregulation of Cdc42 protein signal transduction
H0033668biological_processsymbiont-mediated suppression of host apoptosis
H0039502biological_processsymbiont-mediated suppression of host type I interferon-mediated signaling pathway
H0039548biological_processsymbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity
H0039648biological_processsymbiont-mediated perturbation of host ubiquitin-like protein modification
H0039653biological_processsymbiont-mediated suppression of host transcription
H0042025cellular_componenthost cell nucleus
H0042802molecular_functionidentical protein binding
H0045944biological_processpositive regulation of transcription by RNA polymerase II
H0046872molecular_functionmetal ion binding
H0052150biological_processsymbiont-mediated perturbation of host apoptosis
H0052170biological_processsymbiont-mediated suppression of host innate immune response
H0060255biological_processregulation of macromolecule metabolic process
H0080090biological_processregulation of primary metabolic process
Functional Information from PROSITE/UniProt
site_idPS00348
Number of Residues13
DetailsP53 p53 family signature. MCNSSCMGGMNRR
ChainResidueDetails
CMET237-ARG249
site_idPS01037
Number of Residues18
DetailsSBP_BACTERIAL_1 Bacterial extracellular solute-binding proteins, family 1 signature. PIAvEalSLIYNkdlLpN
ChainResidueDetails
APRO108-ASN125
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues380
DetailsDNA binding: {"evidences":[{"source":"PubMed","id":"16793544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18996393","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20364130","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues246
DetailsRegion: {"description":"Required for interaction with FBXO42","evidences":[{"source":"PubMed","id":"19509332","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues352
DetailsRegion: {"description":"Interaction with AXIN1","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues14
DetailsRegion: {"description":"Interaction with the 53BP2 SH3 domain"}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues14
DetailsRegion: {"description":"Interaction with DNA"}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"14534297","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16793544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17015838","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18650397","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19515728","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20142040","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20364130","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsSite: {"description":"Interaction with DNA","evidences":[{"source":"PubMed","id":"16793544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18996393","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20364130","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues4
DetailsModified residue: {"description":"N6-lactoyllysine","evidences":[{"source":"PubMed","id":"38653238","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine; by AURKB","evidences":[{"source":"PubMed","id":"20959462","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine; by AURKB","evidences":[{"source":"PubMed","id":"20959462","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues6
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"19536131","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues144
DetailsZinc finger: {"evidences":[{"source":"HAMAP-Rule","id":"MF_04006","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues2
DetailsMotif: {"description":"PDZ-binding domain","evidences":[{"source":"HAMAP-Rule","id":"MF_04006","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idMCSA1
Number of Residues
DetailsM-CSA 438
ChainResidueDetails
site_idMCSA2
Number of Residues
DetailsM-CSA 438
ChainResidueDetails

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PDB entries from 2025-07-16

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