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4F6W

Crystal structure of human CDK8/CYCC in complex with compound 1 (N-[3-tert-butyl-1-(4-methylphenyl)-1H-pyrazol-5-yl]-4-[2-({[3-tert-butyl-1-(4-methylphenyl)-1H-pyrazol-5-yl]carbamoyl}amino)ethyl]piperazine-1-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 Residues16
DetailsBINDING SITE FOR RESIDUE 0SS A 501
ChainResidue
AVAL27
AASP173
AMET174
AARG356
AHOH603
AHOH614
AHOH633
AHOH649
ATYR32
ASER62
AGLU66
AILE79
APHE97
ATRP105
AHIS149
AALA172

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE DMS A 502
ChainResidue
ALYS153
AHOH608

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO A 503
ChainResidue
ASER343

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO A 504
ChainResidue
ALYS307

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 505
ChainResidue
APRO124
AGLY126
AMET127

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 506
ChainResidue
AARG13
AGLU14
AVAL84
APHE85

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE FMT A 507
ChainResidue
AVAL84
BASP147

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FMT A 508
ChainResidue
AGLU21
ATYR22
AGLU23

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 301
ChainResidue
BALA0
BALA2
BVAL152
BTYR153

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 302
ChainResidue
BGLN49
BGLU53
BLEU57
BGLN59

site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO B 303
ChainResidue
BGLN161
BTYR162

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 304
ChainResidue
ALEU9
BTYR76
BTYR141
BGLU144
BLEU145

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 305
ChainResidue
ATHR57
AILE59
BPHE92
BLYS96
BHOH422
BHOH438

site_idBC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FMT B 306
ChainResidue
BASN46
BARG185
BGLU246

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT B 307
ChainResidue
BGLN41
BTHR45
BTHR66
BPHE69
BLYS70
BTYR184

site_idBC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT B 308
ChainResidue
BTHR118
BARG119
BPHE120
BSER121
BARG247

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

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PDB entries from 2024-06-12

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