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6GU2

CDK1/CyclinB/Cks2 in complex with Flavopiridol

Functional Information from GO Data
ChainGOidnamespacecontents
A0000082biological_processG1/S transition of mitotic cell cycle
A0000086biological_processG2/M transition of mitotic cell cycle
A0000166molecular_functionnucleotide binding
A0000226biological_processmicrotubule cytoskeleton organization
A0000307cellular_componentcyclin-dependent protein kinase holoenzyme complex
A0000781cellular_componentchromosome, telomeric region
A0001618molecular_functionvirus receptor activity
A0003682molecular_functionchromatin binding
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004693molecular_functioncyclin-dependent protein serine/threonine kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0005789cellular_componentendoplasmic reticulum membrane
A0005813cellular_componentcentrosome
A0005819cellular_componentspindle
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005876cellular_componentspindle microtubule
A0006260biological_processDNA replication
A0006281biological_processDNA repair
A0006338biological_processchromatin remodeling
A0006357biological_processregulation of transcription by RNA polymerase II
A0006468biological_processprotein phosphorylation
A0006915biological_processapoptotic process
A0007049biological_processcell cycle
A0007077biological_processmitotic nuclear membrane disassembly
A0007095biological_processmitotic G2 DNA damage checkpoint signaling
A0007098biological_processcentrosome cycle
A0007344biological_processpronuclear fusion
A0008353molecular_functionRNA polymerase II CTD heptapeptide repeat kinase activity
A0009410biological_processresponse to xenobiotic stimulus
A0009636biological_processresponse to toxic substance
A0010243biological_processresponse to organonitrogen compound
A0010628biological_processpositive regulation of gene expression
A0010629biological_processnegative regulation of gene expression
A0010971biological_processpositive regulation of G2/M transition of mitotic cell cycle
A0014038biological_processregulation of Schwann cell differentiation
A0014070biological_processresponse to organic cyclic compound
A0014075biological_processresponse to amine
A0014823biological_processresponse to activity
A0016020cellular_componentmembrane
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0016477biological_processcell migration
A0016740molecular_functiontransferase activity
A0018105biological_processpeptidyl-serine phosphorylation
A0018107biological_processpeptidyl-threonine phosphorylation
A0030261biological_processchromosome condensation
A0030332molecular_functioncyclin binding
A0030496cellular_componentmidbody
A0030544molecular_functionHsp70 protein binding
A0030855biological_processepithelial cell differentiation
A0031100biological_processanimal organ regeneration
A0034501biological_processprotein localization to kinetochore
A0035173molecular_functionhistone kinase activity
A0042307biological_processpositive regulation of protein import into nucleus
A0042542biological_processresponse to hydrogen peroxide
A0042752biological_processregulation of circadian rhythm
A0043066biological_processnegative regulation of apoptotic process
A0044772biological_processmitotic cell cycle phase transition
A0045471biological_processresponse to ethanol
A0045740biological_processpositive regulation of DNA replication
A0045931biological_processpositive regulation of mitotic cell cycle
A0045995biological_processregulation of embryonic development
A0046686biological_processresponse to cadmium ion
A0046688biological_processresponse to copper ion
A0046718biological_processsymbiont entry into host cell
A0048144biological_processfibroblast proliferation
A0048511biological_processrhythmic process
A0048678biological_processresponse to axon injury
A0051301biological_processcell division
A0055015biological_processventricular cardiac muscle cell development
A0060045biological_processpositive regulation of cardiac muscle cell proliferation
A0062033biological_processpositive regulation of mitotic sister chromatid segregation
A0065003biological_processprotein-containing complex assembly
A0070062cellular_componentextracellular exosome
A0070301biological_processcellular response to hydrogen peroxide
A0070371biological_processERK1 and ERK2 cascade
A0071407biological_processcellular response to organic cyclic compound
A0072686cellular_componentmitotic spindle
A0090166biological_processGolgi disassembly
A0097122cellular_componentcyclin A2-CDK1 complex
A0097125cellular_componentcyclin B1-CDK1 complex
A0097472molecular_functioncyclin-dependent protein kinase activity
A0106310molecular_functionprotein serine kinase activity
A1900182biological_processpositive regulation of protein localization to nucleus
A1902850biological_processmicrotubule cytoskeleton organization involved in mitosis
A1905448biological_processpositive regulation of mitochondrial ATP synthesis coupled electron transport
B0016538molecular_functioncyclin-dependent protein serine/threonine kinase regulator activity
B0044772biological_processmitotic cell cycle phase transition
C0016538molecular_functioncyclin-dependent protein serine/threonine kinase regulator activity
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue F9Z A 301
ChainResidue
AVAL18
ALEU135
AASP146
AHOH403
AALA31
ALYS33
AVAL64
APHE80
AGLU81
APHE82
ALEU83
ASER84

Functional Information from PROSITE/UniProt
site_idPS00944
Number of Residues19
DetailsCKS_1 Cyclin-dependent kinases regulatory subunits signature 1. YSdKYfDEhYEYRHVmLPR
ChainResidueDetails
CTYR8-ARG26

site_idPS00945
Number of Residues11
DetailsCKS_2 Cyclin-dependent kinases regulatory subunits signature 2. HePEpHILLFR
ChainResidueDetails
CHIS60-ARG70

site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGTYGVVYkGrhkttgqv..........VAMK
ChainResidueDetails
AILE10-LYS33

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpqNLLI
ChainResidueDetails
AVAL124-ILE136

site_idPS00292
Number of Residues32
DetailsCYCLINS Cyclins signature. RaiLidWLvqvqmkfrLlqetMymTVsIIDRF
ChainResidueDetails
BARG201-PHE232

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
CLYS4

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AILE10
ALYS33

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:22814378
ChainResidueDetails
AMET1

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by PKR => ECO:0000269|PubMed:20395957
ChainResidueDetails
ATYR4

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS6

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P11440
ChainResidueDetails
ALYS9

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by PKMYT1 => ECO:0000269|PubMed:7569953, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332
ChainResidueDetails
ATHR14

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by PKMYT1, WEE1, WEE2 and PKC/PRKCD => ECO:0000269|PubMed:19917613, ECO:0000269|PubMed:29606300, ECO:0000269|PubMed:7569953, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332
ChainResidueDetails
ATYR15

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195
ChainResidueDetails
ATYR19

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER39

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18691976
ChainResidueDetails
ATYR77

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR141

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by CAK => ECO:0000269|PubMed:20360007, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR161

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195
ChainResidueDetails
ASER178
ASER248

site_idSWS_FT_FI15
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195
ChainResidueDetails
ATHR222

site_idSWS_FT_FI16
Number of Residues1
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P11440
ChainResidueDetails
ALYS245

site_idSWS_FT_FI17
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS6
ALYS9

site_idSWS_FT_FI18
Number of Residues3
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS20
ALYS139

218853

PDB entries from 2024-04-24

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