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1FQ1

CRYSTAL STRUCTURE OF KINASE ASSOCIATED PHOSPHATASE (KAP) IN COMPLEX WITH PHOSPHO-CDK2

Functional Information from GO Data
ChainGOidnamespacecontents
A0000079biological_processregulation of cyclin-dependent protein serine/threonine kinase activity
A0000082biological_processG1/S transition of mitotic cell cycle
A0004721molecular_functionphosphoprotein phosphatase activity
A0004722molecular_functionprotein serine/threonine phosphatase activity
A0004725molecular_functionprotein tyrosine phosphatase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006470biological_processprotein dephosphorylation
A0007049biological_processcell cycle
A0008138molecular_functionprotein tyrosine/serine/threonine phosphatase activity
A0008285biological_processnegative regulation of cell population proliferation
A0016311biological_processdephosphorylation
A0016787molecular_functionhydrolase activity
A0017018molecular_functionmyosin phosphatase activity
A0048471cellular_componentperinuclear region of cytoplasm
A0051726biological_processregulation of cell cycle
B0000082biological_processG1/S transition of mitotic cell cycle
B0000086biological_processG2/M transition of mitotic cell cycle
B0000122biological_processnegative regulation of transcription by RNA polymerase II
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0000307cellular_componentcyclin-dependent protein kinase holoenzyme complex
B0000781cellular_componentchromosome, telomeric region
B0000793cellular_componentcondensed chromosome
B0000805cellular_componentX chromosome
B0000806cellular_componentY chromosome
B0001673cellular_componentmale germ cell nucleus
B0004672molecular_functionprotein kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0004693molecular_functioncyclin-dependent protein serine/threonine kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005635cellular_componentnuclear envelope
B0005654cellular_componentnucleoplasm
B0005667cellular_componenttranscription regulator complex
B0005737cellular_componentcytoplasm
B0005768cellular_componentendosome
B0005813cellular_componentcentrosome
B0005829cellular_componentcytosol
B0005856cellular_componentcytoskeleton
B0006260biological_processDNA replication
B0006281biological_processDNA repair
B0006338biological_processchromatin remodeling
B0006351biological_processDNA-templated transcription
B0006468biological_processprotein phosphorylation
B0006813biological_processpotassium ion transport
B0006974biological_processDNA damage response
B0007049biological_processcell cycle
B0007099biological_processcentriole replication
B0007165biological_processsignal transduction
B0007265biological_processRas protein signal transduction
B0007346biological_processregulation of mitotic cell cycle
B0008284biological_processpositive regulation of cell population proliferation
B0010033biological_processresponse to organic substance
B0010389biological_processregulation of G2/M transition of mitotic cell cycle
B0010468biological_processregulation of gene expression
B0015030cellular_componentCajal body
B0016301molecular_functionkinase activity
B0016310biological_processphosphorylation
B0016740molecular_functiontransferase activity
B0018105biological_processpeptidyl-serine phosphorylation
B0019904molecular_functionprotein domain specific binding
B0030332molecular_functioncyclin binding
B0031453biological_processpositive regulation of heterochromatin formation
B0031571biological_processmitotic G1 DNA damage checkpoint signaling
B0032298biological_processpositive regulation of DNA-templated DNA replication initiation
B0035173molecular_functionhistone kinase activity
B0043687biological_processpost-translational protein modification
B0045740biological_processpositive regulation of DNA replication
B0045893biological_processpositive regulation of DNA-templated transcription
B0046872molecular_functionmetal ion binding
B0051298biological_processcentrosome duplication
B0051301biological_processcell division
B0051321biological_processmeiotic cell cycle
B0071732biological_processcellular response to nitric oxide
B0090398biological_processcellular senescence
B0097123cellular_componentcyclin A1-CDK2 complex
B0097124cellular_componentcyclin A2-CDK2 complex
B0097134cellular_componentcyclin E1-CDK2 complex
B0097135cellular_componentcyclin E2-CDK2 complex
B0097472molecular_functioncyclin-dependent protein kinase activity
B0106310molecular_functionprotein serine kinase activity
B1905784biological_processregulation of anaphase-promoting complex-dependent catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG B 383
ChainResidue
BASN132
BASP145
BATP381

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ATP B 381
ChainResidue
BGLU81
BPHE82
BLEU83
BASP86
BLYS89
BASP127
BLYS129
BGLN131
BASN132
BASP145
BMG383
BILE10
BGLY13
BTHR14
BVAL18
BALA31
BLYS33

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGTYGVVYkArnkltgev..........VALK
ChainResidueDetails
BILE10-LYS33

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpqNLLI
ChainResidueDetails
BVAL123-ILE135

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
BASP127

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702
ChainResidueDetails
BLYS33
BGLU81
BASP86
BLYS129
BILE10

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:21565702
ChainResidueDetails
BASN132
BASP145

site_idSWS_FT_FI4
Number of Residues3
DetailsSITE: CDK7 binding
ChainResidueDetails
BLYS9
BLYS88
BLEU166

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22814378
ChainResidueDetails
BMET1

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
BLYS6

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:1396589, ECO:0000269|PubMed:17095507
ChainResidueDetails
BTHR14

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by WEE1 => ECO:0000269|PubMed:1396589, ECO:0000269|PubMed:17095507, ECO:0007744|PubMed:19690332
ChainResidueDetails
BTYR15

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19369195
ChainResidueDetails
BTYR19

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by CAK and CCRK => ECO:0000269|PubMed:1396589, ECO:0000269|PubMed:14597612, ECO:0000269|PubMed:16325401, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:17570665, ECO:0000269|PubMed:20147522, ECO:0000269|PubMed:20360007, ECO:0000269|PubMed:21565702, ECO:0000305|PubMed:28666995
ChainResidueDetails
BTPO160

218500

数据于2024-04-17公开中

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