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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7U5C

Cryo-EM structure of human CST bound to DNA polymerase alpha-primase in a recruitment state

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0000428cellular_componentDNA-directed RNA polymerase complex
A0003899molecular_functionDNA-directed RNA polymerase activity
A0005515molecular_functionprotein binding
A0005654cellular_componentnucleoplasm
A0005658cellular_componentalpha DNA polymerase:primase complex
A0006260biological_processDNA replication
A0006269biological_processDNA replication, synthesis of primer
A0006270biological_processDNA replication initiation
A0008270molecular_functionzinc ion binding
A0016020cellular_componentmembrane
A0016740molecular_functiontransferase activity
A0016779molecular_functionnucleotidyltransferase activity
A0032553molecular_functionribonucleotide binding
A0046872molecular_functionmetal ion binding
B0003677molecular_functionDNA binding
B0003899molecular_functionDNA-directed RNA polymerase activity
B0005515molecular_functionprotein binding
B0005654cellular_componentnucleoplasm
B0005658cellular_componentalpha DNA polymerase:primase complex
B0006260biological_processDNA replication
B0006269biological_processDNA replication, synthesis of primer
B0006270biological_processDNA replication initiation
B0046872molecular_functionmetal ion binding
B0051536molecular_functioniron-sulfur cluster binding
B0051539molecular_function4 iron, 4 sulfur cluster binding
B0071667molecular_functionDNA/RNA hybrid binding
C0000166molecular_functionnucleotide binding
C0003676molecular_functionnucleic acid binding
C0003677molecular_functionDNA binding
C0003887molecular_functionDNA-directed DNA polymerase activity
C0006260biological_processDNA replication
C1902975biological_processmitotic DNA replication initiation
D0003677molecular_functionDNA binding
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005658cellular_componentalpha DNA polymerase:primase complex
D0005829cellular_componentcytosol
D0006260biological_processDNA replication
D0006269biological_processDNA replication, synthesis of primer
D0006270biological_processDNA replication initiation
D0006606biological_processprotein import into nucleus
D0036064cellular_componentciliary basal body
E0000723biological_processtelomere maintenance
E0000781cellular_componentchromosome, telomeric region
E0003677molecular_functionDNA binding
E0003697molecular_functionsingle-stranded DNA binding
E0005515molecular_functionprotein binding
E0005634cellular_componentnucleus
E0005654cellular_componentnucleoplasm
E0005829cellular_componentcytosol
E0006974biological_processDNA damage response
E0010389biological_processregulation of G2/M transition of mitotic cell cycle
E0010833biological_processtelomere maintenance via telomere lengthening
E0016233biological_processtelomere capping
E0032211biological_processnegative regulation of telomere maintenance via telomerase
E0035264biological_processmulticellular organism growth
E0042162molecular_functiontelomeric DNA binding
E0045740biological_processpositive regulation of DNA replication
E0048146biological_processpositive regulation of fibroblast proliferation
E0048536biological_processspleen development
E0048538biological_processthymus development
E0048539biological_processbone marrow development
E0051276biological_processchromosome organization
E0071425biological_processhematopoietic stem cell proliferation
E0090399biological_processreplicative senescence
E0098505molecular_functionG-rich strand telomeric DNA binding
E1990879cellular_componentCST complex
F0000723biological_processtelomere maintenance
F0000781cellular_componentchromosome, telomeric region
F0001650cellular_componentfibrillar center
F0003676molecular_functionnucleic acid binding
F0003677molecular_functionDNA binding
F0003697molecular_functionsingle-stranded DNA binding
F0005515molecular_functionprotein binding
F0005634cellular_componentnucleus
F0005654cellular_componentnucleoplasm
F0010833biological_processtelomere maintenance via telomere lengthening
F0016233biological_processtelomere capping
F0032211biological_processnegative regulation of telomere maintenance via telomerase
F0042162molecular_functiontelomeric DNA binding
F0043047molecular_functionsingle-stranded telomeric DNA binding
F0045111cellular_componentintermediate filament cytoskeleton
F0045740biological_processpositive regulation of DNA replication
F0051052biological_processregulation of DNA metabolic process
F1990879cellular_componentCST complex
G0000781cellular_componentchromosome, telomeric region
G0003677molecular_functionDNA binding
G0003697molecular_functionsingle-stranded DNA binding
G0005515molecular_functionprotein binding
G0005634cellular_componentnucleus
G0005654cellular_componentnucleoplasm
G0010521molecular_functiontelomerase inhibitor activity
G0016233biological_processtelomere capping
G0032211biological_processnegative regulation of telomere maintenance via telomerase
G0042162molecular_functiontelomeric DNA binding
G1990879cellular_componentCST complex
Functional Information from PROSITE/UniProt
site_idPS00116
Number of Residues9
DetailsDNA_POLYMERASE_B DNA polymerase family B signature. YGDTDSIMI
ChainResidueDetails
CTYR1000-ILE1008
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsMotif: {"description":"Zinc knuckle motif","evidences":[{"source":"PubMed","id":"24043831","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25550159","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26975377","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues3
DetailsActive site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24043831","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31479243","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"31479243","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6R4S","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24043831","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25550159","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26975377","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31479243","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24043831","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24239947","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31479243","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"31479243","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues17
DetailsRegion: {"description":"Interdomain linker","evidences":[{"source":"PubMed","id":"25550159","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26975377","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues142
DetailsRegion: {"description":"RNA:DNA duplex-binding","evidences":[{"source":"PubMed","id":"26975377","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17893144","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25550159","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26975377","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17893144","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25550159","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues35
DetailsZinc finger: {"description":"CysA-type","evidences":[{"source":"UniProtKB","id":"P15436","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues26
DetailsMotif: {"description":"CysB motif","evidences":[{"source":"UniProtKB","id":"P15436","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"26975377","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5EXR","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P33609","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

244349

PDB entries from 2025-11-05

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