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2W99

Crystal Structure of CDK4 in complex with a D-type cyclin

Functional Information from GO Data
ChainGOidnamespacecontents
A0000082biological_processG1/S transition of mitotic cell cycle
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0000307cellular_componentcyclin-dependent protein kinase holoenzyme complex
A0001889biological_processliver development
A0003714molecular_functiontranscription corepressor activity
A0004672molecular_functionprotein kinase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005815cellular_componentmicrotubule organizing center
A0005829cellular_componentcytosol
A0005923cellular_componentbicellular tight junction
A0006351biological_processDNA-templated transcription
A0006357biological_processregulation of transcription by RNA polymerase II
A0006974biological_processDNA damage response
A0008284biological_processpositive regulation of cell population proliferation
A0009410biological_processresponse to xenobiotic stimulus
A0010039biological_processresponse to iron ion
A0010165biological_processresponse to X-ray
A0010971biological_processpositive regulation of G2/M transition of mitotic cell cycle
A0016301molecular_functionkinase activity
A0016538molecular_functioncyclin-dependent protein serine/threonine kinase regulator activity
A0017053cellular_componenttranscription repressor complex
A0019899molecular_functionenzyme binding
A0019901molecular_functionprotein kinase binding
A0031100biological_processanimal organ regeneration
A0031571biological_processmitotic G1 DNA damage checkpoint signaling
A0031965cellular_componentnuclear membrane
A0032026biological_processresponse to magnesium ion
A0032355biological_processresponse to estradiol
A0033197biological_processresponse to vitamin E
A0033327biological_processLeydig cell differentiation
A0042826molecular_functionhistone deacetylase binding
A0043539molecular_functionprotein serine/threonine kinase activator activity
A0043627biological_processresponse to estrogen
A0044321biological_processresponse to leptin
A0044877molecular_functionprotein-containing complex binding
A0045471biological_processresponse to ethanol
A0048545biological_processresponse to steroid hormone
A0051301biological_processcell division
A0051384biological_processresponse to glucocorticoid
A0051412biological_processresponse to corticosterone
A0051592biological_processresponse to calcium ion
A0061575molecular_functioncyclin-dependent protein serine/threonine kinase activator activity
A0070064molecular_functionproline-rich region binding
A0070141biological_processresponse to UV-A
A0071456biological_processcellular response to hypoxia
A1900087biological_processpositive regulation of G1/S transition of mitotic cell cycle
A1901992biological_processpositive regulation of mitotic cell cycle phase transition
A2000045biological_processregulation of G1/S transition of mitotic cell cycle
B0000082biological_processG1/S transition of mitotic cell cycle
B0000086biological_processG2/M transition of mitotic cell cycle
B0000166molecular_functionnucleotide binding
B0000307cellular_componentcyclin-dependent protein kinase holoenzyme complex
B0000785cellular_componentchromatin
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
B0005667cellular_componenttranscription regulator complex
B0005730cellular_componentnucleolus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005923cellular_componentbicellular tight junction
B0006468biological_processprotein phosphorylation
B0007165biological_processsignal transduction
B0008284biological_processpositive regulation of cell population proliferation
B0009410biological_processresponse to xenobiotic stimulus
B0010468biological_processregulation of gene expression
B0010971biological_processpositive regulation of G2/M transition of mitotic cell cycle
B0016301molecular_functionkinase activity
B0016538molecular_functioncyclin-dependent protein serine/threonine kinase regulator activity
B0016740molecular_functiontransferase activity
B0030332molecular_functioncyclin binding
B0031965cellular_componentnuclear membrane
B0048146biological_processpositive regulation of fibroblast proliferation
B0051301biological_processcell division
B0051726biological_processregulation of cell cycle
B0060260biological_processregulation of transcription initiation by RNA polymerase II
B0097128cellular_componentcyclin D1-CDK4 complex
B0097129cellular_componentcyclin D2-CDK4 complex
B0106310molecular_functionprotein serine kinase activity
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGVGAYGTVYkArdphsghf..........VALK
ChainResidueDetails
BILE12-LYS35

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDLKpeNILV
ChainResidueDetails
BILE136-VAL148

site_idPS00292
Number of Residues32
DetailsCYCLINS Cyclins signature. RkiVatWMlevceeqkCeeevFplAMnYLDRF
ChainResidueDetails
AARG57-PHE88

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues124
DetailsDomain: {"description":"Cyclin N-terminal"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsRegion: {"description":"Required for binding D-type cyclins"}
ChainResidueDetails

site_idSWS_FT_FI3
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_FI4
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"16782892","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19237555","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19237565","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19487459","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP140
BGLU144

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BLYS142
BASP140

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BLYS142
BTHR177
BASP140

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BLYS142
BASN145
BASP140

246704

PDB entries from 2025-12-24

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