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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

1UA2

Crystal Structure of Human CDK7

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000439cellular_componenttranscription factor TFIIH core complex
A0001650cellular_componentfibrillar center
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
A0005675cellular_componenttranscription factor TFIIH holo complex
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006281biological_processDNA repair
A0006289biological_processnucleotide-excision repair
A0006351biological_processDNA-templated transcription
A0006366biological_processtranscription by RNA polymerase II
A0006367biological_processtranscription initiation at RNA polymerase II promoter
A0006468biological_processprotein phosphorylation
A0006974biological_processDNA damage response
A0008094molecular_functionATP-dependent activity, acting on DNA
A0008353molecular_functionRNA polymerase II CTD heptapeptide repeat kinase activity
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0042795biological_processsnRNA transcription by RNA polymerase II
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0048471cellular_componentperinuclear region of cytoplasm
A0050821biological_processprotein stabilization
A0051301biological_processcell division
A0051726biological_processregulation of cell cycle
A0070516cellular_componentCAK-ERCC2 complex
A0070985cellular_componenttranscription factor TFIIK complex
A0106310molecular_functionprotein serine kinase activity
A0140836molecular_functionRNA polymerase II CTD heptapeptide repeat S5 kinase activity
A2000045biological_processregulation of G1/S transition of mitotic cell cycle
B0000166molecular_functionnucleotide binding
B0000439cellular_componenttranscription factor TFIIH core complex
B0001650cellular_componentfibrillar center
B0004672molecular_functionprotein kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0004693molecular_functioncyclin-dependent protein serine/threonine kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005675cellular_componenttranscription factor TFIIH holo complex
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006281biological_processDNA repair
B0006289biological_processnucleotide-excision repair
B0006351biological_processDNA-templated transcription
B0006366biological_processtranscription by RNA polymerase II
B0006367biological_processtranscription initiation at RNA polymerase II promoter
B0006468biological_processprotein phosphorylation
B0006974biological_processDNA damage response
B0008094molecular_functionATP-dependent activity, acting on DNA
B0008353molecular_functionRNA polymerase II CTD heptapeptide repeat kinase activity
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0042795biological_processsnRNA transcription by RNA polymerase II
B0045944biological_processpositive regulation of transcription by RNA polymerase II
B0048471cellular_componentperinuclear region of cytoplasm
B0050821biological_processprotein stabilization
B0051301biological_processcell division
B0051726biological_processregulation of cell cycle
B0070516cellular_componentCAK-ERCC2 complex
B0070985cellular_componenttranscription factor TFIIK complex
B0106310molecular_functionprotein serine kinase activity
B0140836molecular_functionRNA polymerase II CTD heptapeptide repeat S5 kinase activity
B2000045biological_processregulation of G1/S transition of mitotic cell cycle
C0000166molecular_functionnucleotide binding
C0000439cellular_componenttranscription factor TFIIH core complex
C0001650cellular_componentfibrillar center
C0004672molecular_functionprotein kinase activity
C0004674molecular_functionprotein serine/threonine kinase activity
C0004693molecular_functioncyclin-dependent protein serine/threonine kinase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005675cellular_componenttranscription factor TFIIH holo complex
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006281biological_processDNA repair
C0006289biological_processnucleotide-excision repair
C0006351biological_processDNA-templated transcription
C0006366biological_processtranscription by RNA polymerase II
C0006367biological_processtranscription initiation at RNA polymerase II promoter
C0006468biological_processprotein phosphorylation
C0006974biological_processDNA damage response
C0008094molecular_functionATP-dependent activity, acting on DNA
C0008353molecular_functionRNA polymerase II CTD heptapeptide repeat kinase activity
C0016301molecular_functionkinase activity
C0016740molecular_functiontransferase activity
C0042795biological_processsnRNA transcription by RNA polymerase II
C0045944biological_processpositive regulation of transcription by RNA polymerase II
C0048471cellular_componentperinuclear region of cytoplasm
C0050821biological_processprotein stabilization
C0051301biological_processcell division
C0051726biological_processregulation of cell cycle
C0070516cellular_componentCAK-ERCC2 complex
C0070985cellular_componenttranscription factor TFIIK complex
C0106310molecular_functionprotein serine kinase activity
C0140836molecular_functionRNA polymerase II CTD heptapeptide repeat S5 kinase activity
C2000045biological_processregulation of G1/S transition of mitotic cell cycle
D0000166molecular_functionnucleotide binding
D0000439cellular_componenttranscription factor TFIIH core complex
D0001650cellular_componentfibrillar center
D0004672molecular_functionprotein kinase activity
D0004674molecular_functionprotein serine/threonine kinase activity
D0004693molecular_functioncyclin-dependent protein serine/threonine kinase activity
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005675cellular_componenttranscription factor TFIIH holo complex
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006281biological_processDNA repair
D0006289biological_processnucleotide-excision repair
D0006351biological_processDNA-templated transcription
D0006366biological_processtranscription by RNA polymerase II
D0006367biological_processtranscription initiation at RNA polymerase II promoter
D0006468biological_processprotein phosphorylation
D0006974biological_processDNA damage response
D0008094molecular_functionATP-dependent activity, acting on DNA
D0008353molecular_functionRNA polymerase II CTD heptapeptide repeat kinase activity
D0016301molecular_functionkinase activity
D0016740molecular_functiontransferase activity
D0042795biological_processsnRNA transcription by RNA polymerase II
D0045944biological_processpositive regulation of transcription by RNA polymerase II
D0048471cellular_componentperinuclear region of cytoplasm
D0050821biological_processprotein stabilization
D0051301biological_processcell division
D0051726biological_processregulation of cell cycle
D0070516cellular_componentCAK-ERCC2 complex
D0070985cellular_componenttranscription factor TFIIK complex
D0106310molecular_functionprotein serine kinase activity
D0140836molecular_functionRNA polymerase II CTD heptapeptide repeat S5 kinase activity
D2000045biological_processregulation of G1/S transition of mitotic cell cycle
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE ATP A 381
ChainResidue
ALEU18
AASP92
APHE93
AMET94
ALYS139
AASN142
ASER161
AGLU20
AGLY21
AGLN22
APHE23
AALA24
AVAL26
AALA39
ALYS41
site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE ATP B 382
ChainResidue
BLEU18
BGLU20
BGLY21
BGLN22
BPHE23
BALA24
BVAL26
BALA39
BLYS41
BPHE91
BASP92
BPHE93
BMET94
BASN142
BSER161
site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ATP C 383
ChainResidue
CGLU20
CGLY21
CGLN22
CPHE23
CALA24
CVAL26
CLYS41
CILE75
CASP92
CMET94
CASN142
CSER161
site_idAC4
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ATP D 384
ChainResidue
DLEU18
DGLU20
DGLY21
DGLN22
DPHE23
DVAL26
DALA39
DLYS41
DILE75
DASP92
DPHE93
DMET94
DASN141
DASN142
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues25
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGQFATVYkArdkntnqiv.........AIKK
ChainResidueDetails
ALEU18-LYS42
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IlHrDLKpnNLLL
ChainResidueDetails
AILE133-LEU145
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
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_FI2
Number of Residues36
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15530371","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues4
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_FI4
Number of Residues4
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
Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASN141
AASP137
site_idCSA10
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BTHR175
BLYS139
BASP137
site_idCSA11
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CTHR175
CLYS139
CASP137
site_idCSA12
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
DTHR175
DLYS139
DASP137
site_idCSA13
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASN142
ALYS139
AASP137
site_idCSA14
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASN142
BLYS139
BASP137
site_idCSA15
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CASN142
CLYS139
CASP137
site_idCSA16
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
DASN142
DLYS139
DASP137
site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASN141
BASP137
site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CASN141
CASP137
site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
DASN141
DASP137
site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ALYS139
AASP137
site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BLYS139
BASP137
site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CLYS139
CASP137
site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
DLYS139
DASP137
site_idCSA9
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ATHR175
ALYS139
AASP137

246333

PDB entries from 2025-12-17

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