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4F7S

Crystal structure of human CDK8/CYCC in the DMG-in conformation

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 Residues11
DetailsBINDING SITE FOR RESIDUE 0SW A 501
ChainResidue
AALA50
ALEU158
AARG356
AILE79
APHE97
AASP98
ATYR99
AALA100
AASP103
AHIS106
AALA155

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 502
ChainResidue
AARG71
BGLN7
BGLN13

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 503
ChainResidue
AARG150
AASP151
ALEU152
AILE215
AASP216
AHOH661
AHOH699

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 504
ChainResidue
AALA177
AARG178
ALEU179
APRO186

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 505
ChainResidue
AVAL302
ALYS303
ASER306

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 506
ChainResidue
ALYS314
AILE324
AGLN328
AASP332
BTRP241
BHOH449

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 507
ChainResidue
ALYS52
AASP173

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 301
ChainResidue
BASP-2
BALA0
BALA2
BARG157

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 302
ChainResidue
BPHE5
BPRO194
BPHE195

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 303
ChainResidue
BGLN49
BGLN59
BALA63
BTYR156
BTYR184
BARG185
BHOH430

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 304
ChainResidue
BILE42
BASN46
BARG185
BGLU246

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 305
ChainResidue
BGLN49
BGLU53
BLEU57
BGLN59

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 306
ChainResidue
ALYS83
AVAL84
BASP147

site_idBC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 307
ChainResidue
BARG58
BGLN59
BGLN60

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT B 308
ChainResidue
BGLN41
BTHR45
BTHR66
BPHE69
BLYS70

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

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PDB entries from 2024-07-17

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