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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

4Y72

Human CDK1/CyclinB1/CKS2 With Inhibitor

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
A0006974biological_processDNA damage response
A0006998biological_processnuclear envelope organization
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
A0009636biological_processresponse to toxic substance
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
A0014075biological_processresponse to amine
A0014823biological_processresponse to activity
A0016020cellular_componentmembrane
A0016301molecular_functionkinase activity
A0016477biological_processcell migration
A0016579biological_processprotein deubiquitination
A0016740molecular_functiontransferase activity
A0018107biological_processpeptidyl-threonine phosphorylation
A0030261biological_processchromosome condensation
A0030332molecular_functioncyclin binding
A0030496cellular_componentmidbody
A0030544molecular_functionHsp70 protein binding
A0030855biological_processepithelial cell differentiation
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
A0045995biological_processregulation of embryonic development
A0046105biological_processthymidine biosynthetic process
A0046686biological_processresponse to cadmium ion
A0046688biological_processresponse to copper ion
A0046718biological_processsymbiont entry into host cell
A0046785biological_processmicrotubule polymerization
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
A0061523biological_processcilium disassembly
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
A0072686cellular_componentmitotic spindle
A0090166biological_processGolgi disassembly
A0097121cellular_componentcyclin A1-CDK1 complex
A0097122cellular_componentcyclin A2-CDK1 complex
A0097125cellular_componentcyclin B1-CDK1 complex
A0097472molecular_functioncyclin-dependent protein kinase activity
A0106310molecular_functionprotein serine kinase activity
A0110025biological_processDNA strand resection involved in replication fork processing
A1900182biological_processpositive regulation of protein localization to nucleus
A1902423biological_processregulation of attachment of mitotic spindle microtubules to kinetochore
A1902850biological_processmicrotubule cytoskeleton organization involved in mitosis
A1904860biological_processDNA synthesis involved in mitotic DNA replication
A1905448biological_processpositive regulation of mitochondrial ATP synthesis coupled electron transport
A1990166biological_processprotein localization to site of double-strand break
A1990506biological_processmitotic DNA-templated DNA replication
B0016538molecular_functioncyclin-dependent protein serine/threonine kinase regulator activity
B0044772biological_processmitotic cell cycle phase transition
C0000307cellular_componentcyclin-dependent protein kinase holoenzyme complex
C0003682molecular_functionchromatin binding
C0005515molecular_functionprotein binding
C0006357biological_processregulation of transcription by RNA polymerase II
C0007127biological_processmeiosis I
C0007346biological_processregulation of mitotic cell cycle
C0016538molecular_functioncyclin-dependent protein serine/threonine kinase regulator activity
C0019005cellular_componentSCF ubiquitin ligase complex
C0019901molecular_functionprotein kinase binding
C0042393molecular_functionhistone binding
C0043130molecular_functionubiquitin binding
C0044772biological_processmitotic cell cycle phase transition
C0048144biological_processfibroblast proliferation
C0051301biological_processcell division
C0061575molecular_functioncyclin-dependent protein serine/threonine kinase activator activity
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue LZ9 A 301
ChainResidue
AILE10
ALYS89
ALEU135
AASP146
AHOH445
AHOH481
ATYR15
AALA31
ALYS33
AGLU81
APHE82
ALEU83
ASER84
AASP86
Functional Information from PROSITE/UniProt
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
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
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues283
DetailsDomain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by PKR","evidences":[{"source":"PubMed","id":"20395957","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P11440","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by PKMYT1","evidences":[{"source":"PubMed","id":"7569953","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by PKMYT1, WEE1, WEE2 and PKC/PRKCD","evidences":[{"source":"PubMed","id":"19917613","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29606300","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7569953","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by CAK","evidences":[{"source":"PubMed","id":"20360007","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P11440","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues3
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues11
DetailsRegion: {"description":"Interaction with CDK2"}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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