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4F6U

Crystal structure of human CDK8/CYCC in complex with compound 5 (1-[3-tert-butyl-1-(4-methylphenyl)-1H-pyrazol-5-yl]-3-[3-(morpholin-4-yl)propyl]urea)

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 Residues14
DetailsBINDING SITE FOR RESIDUE 0SR A 501
ChainResidue
ATYR32
AALA100
AILE171
AALA172
AASP173
AHOH668
AALA50
ASER62
AARG65
AGLU66
ALEU73
AILE79
APHE97
AASP98

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 502
ChainResidue
AHIS75
AASP137
AHIS140
AHOH765

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DMS A 503
ChainResidue
APRO164
AARG166
AARG168
ASER343

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 504
ChainResidue
AARG71
AGLU72
BGLN7
BLEU12
BGLN13

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 505
ChainResidue
AHIS249
AASP282
APHE283
ATHR287
ATYR288
AHOH707

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 506
ChainResidue
ALEU70
AARG71
ALEU81
AEDO507
AHOH667

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 507
ChainResidue
AARG71
ALYS83
AVAL84
AEDO506
BASP147

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 508
ChainResidue
APRO124
AGLY126
AMET127

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 509
ChainResidue
AVAL16
AGLU17
ATYR22
AGLN53
ASER87
AASP90
ALYS92
ATRP94

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE FMT A 511
ChainResidue
AARG65
AARG150

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 301
ChainResidue
BALA0
BALA2
BILE151
BVAL152
BTYR153
BHOH442

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 302
ChainResidue
BASN46
BARG185
BTRP241
BPHE244
BGLU246

site_idBC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO B 303
ChainResidue
BGLN161
BTYR162

site_idBC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO B 304
ChainResidue
BASN243

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT B 305
ChainResidue
BGLN41
BTHR45
BTHR66
BLYS70
BTYR184
BFMT307

site_idBC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT B 306
ChainResidue
BHIS54
BLEU55
BARG107
BHOH444

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT B 307
ChainResidue
BTYR37
BGLN41
BFMT305
BHOH478

site_idBC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT B 308
ChainResidue
BLYS126
BGLU127
BPRO129
BHOH506
BHOH513

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
AVAL27
ALYS52

222036

PDB entries from 2024-07-03

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