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5HBH

CDK8-CYCC IN COMPLEX WITH 5-{5-Chloro-4-[1-(2-methoxy-ethyl)-1,8-diaza-spiro[4.5]dec-8-yl]-pyridin-3-yl}-1-methyl-1,3-dihydro-benzo[c]isothiazole 2,2-dioxide

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0000307cellular_componentcyclin-dependent protein kinase holoenzyme complex
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0006357biological_processregulation of transcription by RNA polymerase II
B0016538molecular_functioncyclin-dependent protein serine/threonine kinase regulator activity
B0016592cellular_componentmediator complex
B0042802molecular_functionidentical protein binding
B0045023biological_processG0 to G1 transition
B0045746biological_processnegative regulation of Notch signaling pathway
B0045944biological_processpositive regulation of transcription by RNA polymerase II
B1990508cellular_componentCKM complex
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue 5Y7 A 401
ChainResidue
AVAL27
AHIS106
AALA155
ALEU158
AASP173
APHE176
AARG356
AHOH507
ATYR32
AVAL35
AALA50
ALYS52
APHE97
AASP98
AALA100
AASP103

site_idAC2
Number of Residues4
Detailsbinding site for residue EDO A 402
ChainResidue
AARG150
AASP151
AARG200
ATYR211

site_idAC3
Number of Residues4
Detailsbinding site for residue FMT A 403
ChainResidue
AMET259
AGLN313
ALEU316
BLYS248

site_idAC4
Number of Residues3
Detailsbinding site for residue FMT B 301
ChainResidue
BHIS203
BLYS211
BALA213

site_idAC5
Number of Residues3
Detailsbinding site for residue FMT B 302
ChainResidue
BALA0
BVAL152
BARG157

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues26
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGRGTYGHVYkAkrkdgkddkd........YALK
ChainResidueDetails
AVAL27-LYS52

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpaNILV
ChainResidueDetails
AVAL147-VAL159

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
ChainResidueDetails
AASP151

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AVAL27
ALYS52

218853

PDB entries from 2024-04-24

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