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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9SKQ

Cryo-EM structure of CAK-CDK1-cyclin B1

Functional Information from GO Data
ChainGOidnamespacecontents
A0000082biological_processG1/S transition of mitotic cell cycle
A0000086biological_processG2/M transition of mitotic cell cycle
A0000166molecular_functionnucleotide binding
A0000226biological_processmicrotubule cytoskeleton organization
A0000307cellular_componentcyclin-dependent protein kinase holoenzyme complex
A0000781cellular_componentchromosome, telomeric region
A0001618molecular_functionvirus receptor activity
A0003682molecular_functionchromatin binding
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004693molecular_functioncyclin-dependent protein serine/threonine kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0005789cellular_componentendoplasmic reticulum membrane
A0005813cellular_componentcentrosome
A0005819cellular_componentspindle
A0005829cellular_componentcytosol
A0005876cellular_componentspindle microtubule
A0006260biological_processDNA replication
A0006281biological_processDNA repair
A0006338biological_processchromatin remodeling
A0006357biological_processregulation of transcription by RNA polymerase II
A0006915biological_processapoptotic process
A0006974biological_processDNA damage response
A0007077biological_processmitotic nuclear membrane disassembly
A0007095biological_processmitotic G2 DNA damage checkpoint signaling
A0007098biological_processcentrosome cycle
A0007344biological_processpronuclear fusion
A0008353molecular_functionRNA polymerase II CTD heptapeptide repeat kinase activity
A0009636biological_processresponse to toxic substance
A0010628biological_processpositive regulation of gene expression
A0010971biological_processpositive regulation of G2/M transition of mitotic cell cycle
A0014038biological_processregulation of Schwann cell differentiation
A0014075biological_processresponse to amine
A0014823biological_processresponse to activity
A0016020cellular_componentmembrane
A0016301molecular_functionkinase activity
A0016477biological_processcell migration
A0016579biological_processprotein deubiquitination
A0016740molecular_functiontransferase activity
A0018107biological_processpeptidyl-threonine phosphorylation
A0030261biological_processchromosome condensation
A0030332molecular_functioncyclin binding
A0030496cellular_componentmidbody
A0030544molecular_functionHsp70 protein binding
A0030855biological_processepithelial cell differentiation
A0031397biological_processnegative regulation of protein ubiquitination
A0034501biological_processprotein localization to kinetochore
A0035173molecular_functionhistone kinase activity
A0042307biological_processpositive regulation of protein import into nucleus
A0042542biological_processresponse to hydrogen peroxide
A0042752biological_processregulation of circadian rhythm
A0043066biological_processnegative regulation of apoptotic process
A0045471biological_processresponse to ethanol
A0045740biological_processpositive regulation of DNA replication
A0045995biological_processregulation of embryonic development
A0046686biological_processresponse to cadmium ion
A0046688biological_processresponse to copper ion
A0046718biological_processsymbiont entry into host cell
A0048511biological_processrhythmic process
A0048678biological_processresponse to axon injury
A0051301biological_processcell division
A0055015biological_processventricular cardiac muscle cell development
A0060045biological_processpositive regulation of cardiac muscle cell proliferation
A0062033biological_processpositive regulation of mitotic sister chromatid segregation
A0065003biological_processprotein-containing complex assembly
A0070062cellular_componentextracellular exosome
A0070301biological_processcellular response to hydrogen peroxide
A0070371biological_processERK1 and ERK2 cascade
A0072686cellular_componentmitotic spindle
A0090166biological_processGolgi disassembly
A0097125cellular_componentcyclin B1-CDK1 complex
A0097472molecular_functioncyclin-dependent protein kinase activity
A0106310molecular_functionprotein serine kinase activity
A0120261biological_processregulation of heterochromatin organization
A1900182biological_processpositive regulation of protein localization to nucleus
A1902423biological_processregulation of attachment of mitotic spindle microtubules to kinetochore
A1902850biological_processmicrotubule cytoskeleton organization involved in mitosis
A1905448biological_processpositive regulation of mitochondrial ATP synthesis coupled electron transport
A2000060biological_processpositive regulation of ubiquitin-dependent protein catabolic process
B0000082biological_processG1/S transition of mitotic cell cycle
B0000086biological_processG2/M transition of mitotic cell cycle
B0000922cellular_componentspindle pole
B0000940cellular_componentouter kinetochore
B0001556biological_processoocyte maturation
B0005113molecular_functionpatched binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005759cellular_componentmitochondrial matrix
B0005813cellular_componentcentrosome
B0005815cellular_componentmicrotubule organizing center
B0005829cellular_componentcytosol
B0007052biological_processmitotic spindle organization
B0007080biological_processmitotic metaphase chromosome alignment
B0007283biological_processspermatogenesis
B0009410biological_processresponse to xenobiotic stimulus
B0009612biological_processresponse to mechanical stimulus
B0009636biological_processresponse to toxic substance
B0010629biological_processnegative regulation of gene expression
B0010971biological_processpositive regulation of G2/M transition of mitotic cell cycle
B0016020cellular_componentmembrane
B0016538molecular_functioncyclin-dependent protein serine/threonine kinase regulator activity
B0019901molecular_functionprotein kinase binding
B0031442biological_processpositive regulation of mRNA 3'-end processing
B0042246biological_processtissue regeneration
B0044389molecular_functionubiquitin-like protein ligase binding
B0045931biological_processpositive regulation of mitotic cell cycle
B0046680biological_processresponse to DDT
B0048565biological_processdigestive tract development
B0051301biological_processcell division
B0051987biological_processpositive regulation of attachment of spindle microtubules to kinetochore
B0055015biological_processventricular cardiac muscle cell development
B0060045biological_processpositive regulation of cardiac muscle cell proliferation
B0060623biological_processregulation of chromosome condensation
B0061575molecular_functioncyclin-dependent protein serine/threonine kinase activator activity
B0065003biological_processprotein-containing complex assembly
B0071283biological_processcellular response to iron(III) ion
B0071398biological_processcellular response to fatty acid
B0071456biological_processcellular response to hypoxia
B0090266biological_processregulation of mitotic cell cycle spindle assembly checkpoint
B0097125cellular_componentcyclin B1-CDK1 complex
B1905448biological_processpositive regulation of mitochondrial ATP synthesis coupled electron transport
H0000082biological_processG1/S transition of mitotic cell cycle
H0000439cellular_componenttranscription factor TFIIH core complex
H0005515molecular_functionprotein binding
H0005634cellular_componentnucleus
H0005654cellular_componentnucleoplasm
H0005675cellular_componenttranscription factor TFIIH holo complex
H0006281biological_processDNA repair
H0006289biological_processnucleotide-excision repair
H0006351biological_processDNA-templated transcription
H0006357biological_processregulation of transcription by RNA polymerase II
H0006367biological_processtranscription initiation at RNA polymerase II promoter
H0008270molecular_functionzinc ion binding
H0043066biological_processnegative regulation of apoptotic process
H0046872molecular_functionmetal ion binding
H0048661biological_processpositive regulation of smooth muscle cell proliferation
H0070516cellular_componentCAK-ERCC2 complex
H0070985cellular_componenttranscription factor TFIIK complex
H2000045biological_processregulation of G1/S transition of mitotic cell cycle
I0000307cellular_componentcyclin-dependent protein kinase holoenzyme complex
I0000439cellular_componenttranscription factor TFIIH core complex
I0005515molecular_functionprotein binding
I0005634cellular_componentnucleus
I0005654cellular_componentnucleoplasm
I0005675cellular_componenttranscription factor TFIIH holo complex
I0006289biological_processnucleotide-excision repair
I0006351biological_processDNA-templated transcription
I0006357biological_processregulation of transcription by RNA polymerase II
I0006367biological_processtranscription initiation at RNA polymerase II promoter
I0016251molecular_functionRNA polymerase II general transcription initiation factor activity
I0016301molecular_functionkinase activity
I0016538molecular_functioncyclin-dependent protein serine/threonine kinase regulator activity
I0050821biological_processprotein stabilization
I0070516cellular_componentCAK-ERCC2 complex
I0070985cellular_componenttranscription factor TFIIK complex
I2000045biological_processregulation of G1/S transition of mitotic cell cycle
J0000166molecular_functionnucleotide binding
J0000439cellular_componenttranscription factor TFIIH core complex
J0001650cellular_componentfibrillar center
J0004672molecular_functionprotein kinase activity
J0004674molecular_functionprotein serine/threonine kinase activity
J0004693molecular_functioncyclin-dependent protein serine/threonine kinase activity
J0005515molecular_functionprotein binding
J0005524molecular_functionATP binding
J0005634cellular_componentnucleus
J0005654cellular_componentnucleoplasm
J0005675cellular_componenttranscription factor TFIIH holo complex
J0005737cellular_componentcytoplasm
J0005829cellular_componentcytosol
J0006281biological_processDNA repair
J0006289biological_processnucleotide-excision repair
J0006351biological_processDNA-templated transcription
J0006366biological_processtranscription by RNA polymerase II
J0006367biological_processtranscription initiation at RNA polymerase II promoter
J0006974biological_processDNA damage response
J0008094molecular_functionATP-dependent activity, acting on DNA
J0008353molecular_functionRNA polymerase II CTD heptapeptide repeat kinase activity
J0016301molecular_functionkinase activity
J0016740molecular_functiontransferase activity
J0042795biological_processsnRNA transcription by RNA polymerase II
J0045944biological_processpositive regulation of transcription by RNA polymerase II
J0048471cellular_componentperinuclear region of cytoplasm
J0050821biological_processprotein stabilization
J0051301biological_processcell division
J0051726biological_processregulation of cell cycle
J0070516cellular_componentCAK-ERCC2 complex
J0070985cellular_componenttranscription factor TFIIK complex
J0106310molecular_functionprotein serine kinase activity
J0140836molecular_functionRNA polymerase II CTD heptapeptide repeat S5 kinase activity
J2000045biological_processregulation of G1/S transition of mitotic cell cycle
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues25
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGQFATVYkArdkntnqiv.........AIKK
ChainResidueDetails
JLEU18-LYS42
AILE10-LYS33
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IlHrDLKpnNLLL
ChainResidueDetails
JILE133-LEU145
AVAL124-ILE136
site_idPS00292
Number of Residues32
DetailsCYCLINS Cyclins signature. RaiLidWLvqvqmkfrLlqetMymTVsIIDRF
ChainResidueDetails
BARG202-PHE233
site_idPS00518
Number of Residues10
DetailsZF_RING_1 Zinc finger RING-type signature. CgHtLCesCV
ChainResidueDetails
HCYS26-VAL35
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by CDK8","evidences":[{"source":"PubMed","id":"10993082","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues283
DetailsDomain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15530371","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15530371","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by CDK1 and CDK2","evidences":[{"source":"PubMed","id":"11113184","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9832506","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by CDK2","evidences":[{"source":"PubMed","id":"11113184","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15530371","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9832506","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by PKR","evidences":[{"source":"PubMed","id":"20395957","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P11440","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by PKMYT1","evidences":[{"source":"PubMed","id":"7569953","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by PKMYT1, WEE1, WEE2 and PKC/PRKCD","evidences":[{"source":"PubMed","id":"19917613","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29606300","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7569953","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by CAK","evidences":[{"source":"PubMed","id":"20360007","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P11440","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI24
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
site_idSWS_FT_FI25
Number of Residues3
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues11
DetailsRegion: {"description":"Interaction with CDK2"}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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