Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5XQX

Human CDK8-CYCC in complex with compound 4: N-methyl-4-(4-pyridyl)-1H-pyrrole-2-carboxamide

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 Residues8
Detailsbinding site for residue GOL A 401
ChainResidue
AARG150
AASP151
ALEU152
ATYR199
AILE215
AASP216
AALA219
AHOH513

site_idAC2
Number of Residues9
Detailsbinding site for residue 8CC A 402
ChainResidue
AALA50
ALYS52
APHE97
AASP98
AALA100
ALEU158
AASP173
AHOH501
ATYR32

site_idAC3
Number of Residues4
Detailsbinding site for residue GOL A 403
ChainResidue
AARG71
ALYS83
AVAL84
BASP147

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

PDB statisticsPDBj update infoContact PDBjnumon