Loading
PDBj
English日本語简体中文繁體中文한국어
✖
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help
SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7B5O

Cryo-EM structure of the human CAK bound to ICEC0942 at 2.5 Angstroms resolution

Functional Information from GO Data
ChainGOidnamespacecontents
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
H0045737biological_processpositive regulation of cyclin-dependent protein serine/threonine kinase activity
H0046872molecular_functionmetal ion binding
H0048661biological_processpositive regulation of smooth muscle cell proliferation
H0061575molecular_functioncyclin-dependent protein serine/threonine kinase activator activity
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
J0006468biological_processprotein phosphorylation
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 PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue I74 J 401
ChainResidue
JLEU18
JASP97
JASN141
JLEU144
JHOH509
JHOH528
JVAL26
JALA39
JLYS41
JPHE91
JASP92
JMET94
JGLU95
JTHR96
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues25
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGQFATVYkArdkntnqiv.........AIKK
ChainResidueDetails
JLEU18-LYS42
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IlHrDLKpnNLLL
ChainResidueDetails
JILE133-LEU145
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 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_FI5
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_FI6
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_FI7
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

246704

PDB entries from 2025-12-24

PDB statisticsPDBj update infoContact PDBjnumon