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1JOW

Crystal structure of a complex of human CDK6 and a viral cyclin

Functional Information from GO Data
ChainGOidnamespacecontents
A0000307cellular_componentcyclin-dependent protein kinase holoenzyme complex
A0005737cellular_componentcytoplasm
A0007049biological_processcell cycle
A0016538molecular_functioncyclin-dependent protein serine/threonine kinase regulator activity
A0051301biological_processcell division
B0000082biological_processG1/S transition of mitotic cell cycle
B0000122biological_processnegative regulation of transcription by RNA polymerase II
B0000166molecular_functionnucleotide binding
B0000307cellular_componentcyclin-dependent protein kinase holoenzyme complex
B0001726cellular_componentruffle
B0001954biological_processpositive regulation of cell-matrix adhesion
B0002244biological_processhematopoietic progenitor cell differentiation
B0003323biological_processtype B pancreatic cell development
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
B0005737cellular_componentcytoplasm
B0005813cellular_componentcentrosome
B0005829cellular_componentcytosol
B0005856cellular_componentcytoskeleton
B0006468biological_processprotein phosphorylation
B0007049biological_processcell cycle
B0007165biological_processsignal transduction
B0007219biological_processNotch signaling pathway
B0008285biological_processnegative regulation of cell population proliferation
B0009615biological_processresponse to virus
B0010033biological_processresponse to organic substance
B0010389biological_processregulation of G2/M transition of mitotic cell cycle
B0010468biological_processregulation of gene expression
B0010628biological_processpositive regulation of gene expression
B0014002biological_processastrocyte development
B0016301molecular_functionkinase activity
B0016310biological_processphosphorylation
B0016740molecular_functiontransferase activity
B0021542biological_processdentate gyrus development
B0021670biological_processlateral ventricle development
B0030097biological_processhemopoiesis
B0030154biological_processcell differentiation
B0030332molecular_functioncyclin binding
B0033077biological_processT cell differentiation in thymus
B0042063biological_processgliogenesis
B0042127biological_processregulation of cell population proliferation
B0042995cellular_componentcell projection
B0043697biological_processcell dedifferentiation
B0045596biological_processnegative regulation of cell differentiation
B0045638biological_processnegative regulation of myeloid cell differentiation
B0045646biological_processregulation of erythrocyte differentiation
B0045656biological_processnegative regulation of monocyte differentiation
B0045668biological_processnegative regulation of osteoblast differentiation
B0045786biological_processnegative regulation of cell cycle
B0048146biological_processpositive regulation of fibroblast proliferation
B0048699biological_processgeneration of neurons
B0050680biological_processnegative regulation of epithelial cell proliferation
B0051301biological_processcell division
B0051726biological_processregulation of cell cycle
B0060218biological_processhematopoietic stem cell differentiation
B0097132cellular_componentcyclin D2-CDK6 complex
B0098770molecular_functionFBXO family protein binding
B0106310molecular_functionprotein serine kinase activity
B1902036biological_processregulation of hematopoietic stem cell differentiation
B2000145biological_processregulation of cell motility
B2000773biological_processnegative regulation of cellular senescence
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues25
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGAYGKVFkArdlknggrf.........VALK
ChainResidueDetails
BILE19-LYS43

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VvHrDLKpqNILV
ChainResidueDetails
BVAL141-VAL153

site_idPS00292
Number of Residues32
DetailsCYCLINS Cyclins signature. RtiLltWMhllcesfeLdksvFplSVsILDRY
ChainResidueDetails
AARG52-TYR83

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
BASP145

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
BILE19
BLYS43

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22814378
ChainResidueDetails
BMET1

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455
ChainResidueDetails
BTYR13

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:19369195
ChainResidueDetails
BTYR24

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19369195
ChainResidueDetails
BTHR49
BTHR70

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:11828325
ChainResidueDetails
BTHR177

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
BLYS264

218853

PDB entries from 2024-04-24

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