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7SA0

Crystal structure of CDK2 liganded with compound EF4195

Functional Information from GO Data
ChainGOidnamespacecontents
A0000082biological_processG1/S transition of mitotic cell cycle
A0000086biological_processG2/M transition of mitotic cell cycle
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0000287molecular_functionmagnesium ion binding
A0000307cellular_componentcyclin-dependent protein kinase holoenzyme complex
A0000781cellular_componentchromosome, telomeric region
A0000793cellular_componentcondensed chromosome
A0000805cellular_componentX chromosome
A0000806cellular_componentY chromosome
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
A0005635cellular_componentnuclear envelope
A0005654cellular_componentnucleoplasm
A0005667cellular_componenttranscription regulator complex
A0005737cellular_componentcytoplasm
A0005768cellular_componentendosome
A0005813cellular_componentcentrosome
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0006260biological_processDNA replication
A0006281biological_processDNA repair
A0006338biological_processchromatin remodeling
A0006351biological_processDNA-templated transcription
A0006468biological_processprotein phosphorylation
A0006813biological_processpotassium ion transport
A0007099biological_processcentriole replication
A0007165biological_processsignal transduction
A0007265biological_processRas protein signal transduction
A0007346biological_processregulation of mitotic cell cycle
A0008284biological_processpositive regulation of cell population proliferation
A0010389biological_processregulation of G2/M transition of mitotic cell cycle
A0010468biological_processregulation of gene expression
A0015030cellular_componentCajal body
A0016301molecular_functionkinase activity
A0018105biological_processpeptidyl-serine phosphorylation
A0019904molecular_functionprotein domain specific binding
A0030332molecular_functioncyclin binding
A0031453biological_processpositive regulation of heterochromatin formation
A0031571biological_processmitotic G1 DNA damage checkpoint signaling
A0032298biological_processpositive regulation of DNA-templated DNA replication initiation
A0035173molecular_functionhistone kinase activity
A0043247biological_processtelomere maintenance in response to DNA damage
A0043687biological_processpost-translational protein modification
A0045740biological_processpositive regulation of DNA replication
A0045893biological_processpositive regulation of DNA-templated transcription
A0046872molecular_functionmetal ion binding
A0051298biological_processcentrosome duplication
A0051301biological_processcell division
A0051321biological_processmeiotic cell cycle
A0071732biological_processcellular response to nitric oxide
A0090398biological_processcellular senescence
A0097123cellular_componentcyclin A1-CDK2 complex
A0097124cellular_componentcyclin A2-CDK2 complex
A0097134cellular_componentcyclin E1-CDK2 complex
A0097135cellular_componentcyclin E2-CDK2 complex
A0097472molecular_functioncyclin-dependent protein kinase activity
A0106310molecular_functionprotein serine kinase activity
A1905784biological_processregulation of anaphase-promoting complex-dependent catabolic process
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGTYGVVYkArnkltgev..........VALK
ChainResidueDetails
AILE10-LYS33

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpqNLLI
ChainResidueDetails
AVAL123-ILE135

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AASP127

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702
ChainResidueDetails
AILE10
ALYS33
AGLU81
AASP86
ALYS129

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:21565702
ChainResidueDetails
AASN132
AASP145

site_idSWS_FT_FI4
Number of Residues3
DetailsSITE: CDK7 binding => ECO:0000269|PubMed:17373709
ChainResidueDetails
ALYS9
ALYS88
ALEU166

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22814378
ChainResidueDetails
AMET1

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS6

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:1396589, ECO:0000269|PubMed:17095507
ChainResidueDetails
ATHR14

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by WEE1 => ECO:0000269|PubMed:1396589, ECO:0000269|PubMed:17095507, ECO:0007744|PubMed:19690332
ChainResidueDetails
ATYR15

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19369195
ChainResidueDetails
ATYR19

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by CAK and CCRK => ECO:0000269|PubMed:1396589, ECO:0000269|PubMed:14597612, ECO:0000269|PubMed:16325401, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:17570665, ECO:0000269|PubMed:20147522, ECO:0000269|PubMed:20360007, ECO:0000269|PubMed:21565702, ECO:0000305|PubMed:28666995
ChainResidueDetails
ATHR160

227344

PDB entries from 2024-11-13

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