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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

1OL1

Cyclin A binding groove inhibitor H-Cit-Cit-Leu-Ile-(p-F-Phe)-NH2

Functional Information from GO Data
ChainGOidnamespacecontents
A0000082biological_processG1/S transition of mitotic cell cycle
A0000086biological_processG2/M transition of mitotic cell cycle
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0000307cellular_componentcyclin-dependent protein kinase holoenzyme complex
A0000781cellular_componentchromosome, telomeric region
A0000793cellular_componentcondensed chromosome
A0000805cellular_componentX chromosome
A0000806cellular_componentY chromosome
A0001673cellular_componentmale germ cell nucleus
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
A0005635cellular_componentnuclear envelope
A0005654cellular_componentnucleoplasm
A0005667cellular_componenttranscription regulator complex
A0005737cellular_componentcytoplasm
A0005768cellular_componentendosome
A0005813cellular_componentcentrosome
A0005829cellular_componentcytosol
A0006260biological_processDNA replication
A0006281biological_processDNA repair
A0006338biological_processchromatin remodeling
A0006351biological_processDNA-templated transcription
A0006468biological_processprotein phosphorylation
A0006813biological_processpotassium ion transport
A0006974biological_processDNA damage response
A0007099biological_processcentriole replication
A0007165biological_processsignal transduction
A0007265biological_processRas protein signal transduction
A0007346biological_processregulation of mitotic cell cycle
A0008284biological_processpositive regulation of cell population proliferation
A0010389biological_processregulation of G2/M transition of mitotic cell cycle
A0010468biological_processregulation of gene expression
A0015030cellular_componentCajal body
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0018105biological_processpeptidyl-serine phosphorylation
A0019904molecular_functionprotein domain specific binding
A0030332molecular_functioncyclin binding
A0031453biological_processpositive regulation of heterochromatin formation
A0031571biological_processmitotic G1 DNA damage checkpoint signaling
A0032298biological_processpositive regulation of DNA-templated DNA replication initiation
A0035173molecular_functionhistone kinase activity
A0043247biological_processtelomere maintenance in response to DNA damage
A0043687biological_processpost-translational protein modification
A0045740biological_processpositive regulation of DNA replication
A0045893biological_processpositive regulation of DNA-templated transcription
A0046872molecular_functionmetal ion binding
A0051298biological_processcentrosome duplication
A0051301biological_processcell division
A0051321biological_processmeiotic cell cycle
A0071732biological_processcellular response to nitric oxide
A0090398biological_processcellular senescence
A0097123cellular_componentcyclin A1-CDK2 complex
A0097124cellular_componentcyclin A2-CDK2 complex
A0097134cellular_componentcyclin E1-CDK2 complex
A0097135cellular_componentcyclin E2-CDK2 complex
A0097472molecular_functioncyclin-dependent protein kinase activity
A0106310molecular_functionprotein serine kinase activity
A0120186biological_processnegative regulation of protein localization to chromatin
A0120261biological_processregulation of heterochromatin organization
A1905784biological_processregulation of anaphase-promoting complex-dependent catabolic process
B0016538molecular_functioncyclin-dependent protein serine/threonine kinase regulator activity
B0044772biological_processmitotic cell cycle phase transition
C0000082biological_processG1/S transition of mitotic cell cycle
C0000086biological_processG2/M transition of mitotic cell cycle
C0000122biological_processnegative regulation of transcription by RNA polymerase II
C0000166molecular_functionnucleotide binding
C0000287molecular_functionmagnesium ion binding
C0000307cellular_componentcyclin-dependent protein kinase holoenzyme complex
C0000781cellular_componentchromosome, telomeric region
C0000793cellular_componentcondensed chromosome
C0000805cellular_componentX chromosome
C0000806cellular_componentY chromosome
C0001673cellular_componentmale germ cell nucleus
C0004672molecular_functionprotein kinase activity
C0004674molecular_functionprotein serine/threonine kinase activity
C0004693molecular_functioncyclin-dependent protein serine/threonine kinase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005634cellular_componentnucleus
C0005635cellular_componentnuclear envelope
C0005654cellular_componentnucleoplasm
C0005667cellular_componenttranscription regulator complex
C0005737cellular_componentcytoplasm
C0005768cellular_componentendosome
C0005813cellular_componentcentrosome
C0005829cellular_componentcytosol
C0006260biological_processDNA replication
C0006281biological_processDNA repair
C0006338biological_processchromatin remodeling
C0006351biological_processDNA-templated transcription
C0006468biological_processprotein phosphorylation
C0006813biological_processpotassium ion transport
C0006974biological_processDNA damage response
C0007099biological_processcentriole replication
C0007165biological_processsignal transduction
C0007265biological_processRas protein signal transduction
C0007346biological_processregulation of mitotic cell cycle
C0008284biological_processpositive regulation of cell population proliferation
C0010389biological_processregulation of G2/M transition of mitotic cell cycle
C0010468biological_processregulation of gene expression
C0015030cellular_componentCajal body
C0016301molecular_functionkinase activity
C0016740molecular_functiontransferase activity
C0018105biological_processpeptidyl-serine phosphorylation
C0019904molecular_functionprotein domain specific binding
C0030332molecular_functioncyclin binding
C0031453biological_processpositive regulation of heterochromatin formation
C0031571biological_processmitotic G1 DNA damage checkpoint signaling
C0032298biological_processpositive regulation of DNA-templated DNA replication initiation
C0035173molecular_functionhistone kinase activity
C0043247biological_processtelomere maintenance in response to DNA damage
C0043687biological_processpost-translational protein modification
C0045740biological_processpositive regulation of DNA replication
C0045893biological_processpositive regulation of DNA-templated transcription
C0046872molecular_functionmetal ion binding
C0051298biological_processcentrosome duplication
C0051301biological_processcell division
C0051321biological_processmeiotic cell cycle
C0071732biological_processcellular response to nitric oxide
C0090398biological_processcellular senescence
C0097123cellular_componentcyclin A1-CDK2 complex
C0097124cellular_componentcyclin A2-CDK2 complex
C0097134cellular_componentcyclin E1-CDK2 complex
C0097135cellular_componentcyclin E2-CDK2 complex
C0097472molecular_functioncyclin-dependent protein kinase activity
C0106310molecular_functionprotein serine kinase activity
C0120186biological_processnegative regulation of protein localization to chromatin
C0120261biological_processregulation of heterochromatin organization
C1905784biological_processregulation of anaphase-promoting complex-dependent catabolic process
D0016538molecular_functioncyclin-dependent protein serine/threonine kinase regulator activity
D0044772biological_processmitotic cell cycle phase transition
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR CHAIN F OF CIR-CIR-LEU-ILE-PFF-NH2
ChainResidue
AGLU12
BTYR271
BILE281
BASP283
BTHR285
AGLY13
AVAL163
ATHR165
BMET210
BLEU214
BTRP217
BARG250
BGLN254
site_idAC2
Number of Residues10
DetailsBINDING SITE FOR CHAIN H OF CIR-CIR-LEU-ILE-PFF-NH2
ChainResidue
CASP247
DMET210
DLEU214
DTRP217
DARG250
DGLN254
DILE281
DTHR282
DASP283
DTHR285
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGTYGVVYkArnkltgev..........VALK
ChainResidueDetails
AILE10-LYS33
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpqNLLI
ChainResidueDetails
AVAL123-ILE135
site_idPS00292
Number of Residues32
DetailsCYCLINS Cyclins signature. RaiLvdWLvevgeeykLqnetLhlAVnYIDRF
ChainResidueDetails
BARG211-PHE242
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues564
DetailsDomain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues30
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17095507","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21565702","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21565702","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues6
DetailsSite: {"description":"CDK7 binding","evidences":[{"source":"PubMed","id":"17373709","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"1396589","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17095507","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine; by WEE1","evidences":[{"source":"PubMed","id":"1396589","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17095507","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine; by CAK and CCRK","evidences":[{"source":"PubMed","id":"1396589","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14597612","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16325401","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17095507","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17570665","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20147522","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20360007","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21565702","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28666995","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AGLN131
AASP127
site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CGLN131
CASP127
site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP127
ALYS129
site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CASP127
CLYS129
site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP127
ALYS129
ATHR165
site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CASP127
CLYS129
CTHR165
site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP127
ALYS129
AASN132
site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CASP127
CLYS129
CASN132

243911

PDB entries from 2025-10-29

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