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4CRL

Crystal structure of human CDK8-Cyclin C in complex with cortistatin A

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 Residues9
DetailsBINDING SITE FOR RESIDUE C1I A 1360
ChainResidue
AVAL27
AALA50
AILE79
AASP98
AALA100
ATRP105
AALA155
ALEU158
AARG356

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT A 1361
ChainResidue
APRO124
AGLY126
AMET127
AHOH2070

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 1362
ChainResidue
AGLU101
AHIS102
AGLY161
AGLU162
AILE351

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT A 1363
ChainResidue
ALYS52
AGLU66
APHE97
AASP173

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE FMT B 1265
ChainResidue
BALA74
BARG75

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT B 1266
ChainResidue
BGLN49
BGLN59
BALA63
BTYR156
BTYR184

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
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17525332
ChainResidueDetails
BSER275

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

219869

PDB entries from 2024-05-15

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