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5CEI

Crystal structure of CDK8:Cyclin C complex with compound 22

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0006351biological_processDNA-templated transcription
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 Residues4
Detailsbinding site for residue EDO A 501
ChainResidue
AARG71
AGLU72
BSER9
BGLN13

site_idAC2
Number of Residues1
Detailsbinding site for residue EDO A 502
ChainResidue
ATYR141

site_idAC3
Number of Residues6
Detailsbinding site for residue EDO A 503
ChainResidue
AGLU23
ALYS41
AGLU17
APHE20
AGLU21
ATYR22

site_idAC4
Number of Residues3
Detailsbinding site for residue EDO A 504
ChainResidue
ALYS301
AVAL302
ALYS303

site_idAC5
Number of Residues5
Detailsbinding site for residue FMT A 505
ChainResidue
ALYS52
AGLU66
AALA172
AASP173
A50R508

site_idAC6
Number of Residues3
Detailsbinding site for residue FMT A 506
ChainResidue
AGLU165
AARG166
AARG168

site_idAC7
Number of Residues2
Detailsbinding site for residue FMT A 507
ChainResidue
AARG168
ASER343

site_idAC8
Number of Residues15
Detailsbinding site for residue 50R A 508
ChainResidue
AVAL27
ATYR32
AVAL35
AALA50
ALYS52
AILE79
ATYR99
AALA100
AASP103
AALA155
ALEU158
AASP173
AARG356
AFMT505
AHOH668

site_idAC9
Number of Residues4
Detailsbinding site for residue EDO A 509
ChainResidue
AASP305
AHIS310
BLYS242
BASN243

site_idAD1
Number of Residues1
Detailsbinding site for residue EDO B 301
ChainResidue
BHOH414

site_idAD2
Number of Residues4
Detailsbinding site for residue EDO B 302
ChainResidue
BGLU35
BGLU239
BGLN240
BASN243

site_idAD3
Number of Residues4
Detailsbinding site for residue FMT B 303
ChainResidue
BALA0
BALA2
BVAL152
BARG157

site_idAD4
Number of Residues4
Detailsbinding site for residue FMT B 304
ChainResidue
BPHE31
BSER255
BLYS256
BMET257

site_idAD5
Number of Residues2
Detailsbinding site for residue FMT B 305
ChainResidue
BARG58
BGLN59

site_idAD6
Number of Residues2
Detailsbinding site for residue FMT B 306
ChainResidue
BLEU57
BGLN59

site_idAD7
Number of Residues6
Detailsbinding site for residue EDO B 307
ChainResidue
BILE42
BASN46
BTRP241
BPHE244
BGLU246
BHOH401

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 Residues14
DetailsRegion: {"description":"Interaction with CCNC"}
ChainResidueDetails

site_idSWS_FT_FI2
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_FI3
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues98
DetailsDomain: {"description":"Cyclin N-terminal"}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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