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8R9A

A soakable crystal form of human CDK7 in complex with AMP-PNP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000307cellular_componentcyclin-dependent protein kinase holoenzyme complex
A0000439cellular_componenttranscription factor TFIIH core complex
A0001650cellular_componentfibrillar center
A0001673cellular_componentmale germ cell nucleus
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
A0005886cellular_componentplasma membrane
A0006281biological_processDNA repair
A0006366biological_processtranscription by RNA polymerase II
A0006367biological_processtranscription initiation at RNA polymerase II promoter
A0008094molecular_functionATP-dependent activity, acting on DNA
A0008353molecular_functionRNA polymerase II CTD heptapeptide repeat kinase activity
A0016301molecular_functionkinase 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
A2000045biological_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
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 Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027, ECO:0000269|PubMed:15530371
ChainResidueDetails
AASP137

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:15530371
ChainResidueDetails
ALEU18
ALYS41

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0007744|PubMed:22814378
ChainResidueDetails
AALA2

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976
ChainResidueDetails
ASER7

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine; by CDK1 and CDK2 => ECO:0000269|PubMed:11113184, ECO:0000269|PubMed:9832506, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163
ChainResidueDetails
AASP164

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by CDK2 => ECO:0000269|PubMed:11113184, ECO:0000269|PubMed:15530371, ECO:0000269|PubMed:9832506, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
AGLU170

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231
ChainResidueDetails
ASER321

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PDB entries from 2024-07-17

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