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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8D0K

Human CST-DNA polymerase alpha/primase preinitiation complex bound to 4xTEL-foldback template - PRIM2C advanced PIC

Functional Information from GO Data
ChainGOidnamespacecontents
A0000723biological_processtelomere maintenance
A0000781cellular_componentchromosome, telomeric region
A0003677molecular_functionDNA binding
A0003697molecular_functionsingle-stranded DNA binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0010833biological_processtelomere maintenance via telomere lengthening
A0016233biological_processtelomere capping
A0032211biological_processnegative regulation of telomere maintenance via telomerase
A0042162molecular_functiontelomeric DNA binding
A0045740biological_processpositive regulation of DNA replication
A0098505molecular_functionG-rich strand telomeric DNA binding
A1990879cellular_componentCST complex
B0000723biological_processtelomere maintenance
B0000781cellular_componentchromosome, telomeric region
B0003676molecular_functionnucleic acid binding
B0003677molecular_functionDNA binding
B0003697molecular_functionsingle-stranded DNA binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0010833biological_processtelomere maintenance via telomere lengthening
B0016233biological_processtelomere capping
B0032211biological_processnegative regulation of telomere maintenance via telomerase
B0042162molecular_functiontelomeric DNA binding
B0043047molecular_functionsingle-stranded telomeric DNA binding
B0045740biological_processpositive regulation of DNA replication
B0051052biological_processregulation of DNA metabolic process
B1990879cellular_componentCST complex
C0000781cellular_componentchromosome, telomeric region
C0003677molecular_functionDNA binding
C0003697molecular_functionsingle-stranded DNA binding
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0010521molecular_functiontelomerase inhibitor activity
C0016233biological_processtelomere capping
C0032211biological_processnegative regulation of telomere maintenance via telomerase
C0042162molecular_functiontelomeric DNA binding
C1990879cellular_componentCST complex
D0000287molecular_functionmagnesium ion binding
D0000428cellular_componentDNA-directed RNA polymerase complex
D0003899molecular_functionDNA-directed RNA polymerase activity
D0005515molecular_functionprotein binding
D0005654cellular_componentnucleoplasm
D0005658cellular_componentalpha DNA polymerase:primase complex
D0006260biological_processDNA replication
D0006269biological_processDNA replication, synthesis of primer
D0006270biological_processDNA replication initiation
D0008270molecular_functionzinc ion binding
D0016020cellular_componentmembrane
D0016740molecular_functiontransferase activity
D0016779molecular_functionnucleotidyltransferase activity
D0032553molecular_functionribonucleotide binding
D0046872molecular_functionmetal ion binding
E0003677molecular_functionDNA binding
E0003899molecular_functionDNA-directed RNA polymerase activity
E0005515molecular_functionprotein binding
E0005654cellular_componentnucleoplasm
E0005658cellular_componentalpha DNA polymerase:primase complex
E0006260biological_processDNA replication
E0006269biological_processDNA replication, synthesis of primer
E0006270biological_processDNA replication initiation
E0046872molecular_functionmetal ion binding
E0051536molecular_functioniron-sulfur cluster binding
E0051539molecular_function4 iron, 4 sulfur cluster binding
E0071667molecular_functionDNA/RNA hybrid binding
F0000166molecular_functionnucleotide binding
F0000731biological_processDNA synthesis involved in DNA repair
F0000785cellular_componentchromatin
F0003676molecular_functionnucleic acid binding
F0003677molecular_functionDNA binding
F0003682molecular_functionchromatin binding
F0003688molecular_functionDNA replication origin binding
F0003697molecular_functionsingle-stranded DNA binding
F0003887molecular_functionDNA-directed DNA polymerase activity
F0005515molecular_functionprotein binding
F0005634cellular_componentnucleus
F0005635cellular_componentnuclear envelope
F0005654cellular_componentnucleoplasm
F0005658cellular_componentalpha DNA polymerase:primase complex
F0005730cellular_componentnucleolus
F0005829cellular_componentcytosol
F0006260biological_processDNA replication
F0006261biological_processDNA-templated DNA replication
F0006269biological_processDNA replication, synthesis of primer
F0006270biological_processDNA replication initiation
F0006271biological_processDNA strand elongation involved in DNA replication
F0006272biological_processleading strand elongation
F0006273biological_processlagging strand elongation
F0006281biological_processDNA repair
F0006289biological_processnucleotide-excision repair
F0006303biological_processdouble-strand break repair via nonhomologous end joining
F0008270molecular_functionzinc ion binding
F0016363cellular_componentnuclear matrix
F0016740molecular_functiontransferase activity
F0016779molecular_functionnucleotidyltransferase activity
F0019901molecular_functionprotein kinase binding
F0032479biological_processregulation of type I interferon production
F0034061molecular_functionDNA polymerase activity
F0046872molecular_functionmetal ion binding
F1902975biological_processmitotic DNA replication initiation
F1904161biological_processDNA synthesis involved in UV-damage excision repair
G0003677molecular_functionDNA binding
G0005515molecular_functionprotein binding
G0005634cellular_componentnucleus
G0005654cellular_componentnucleoplasm
G0005658cellular_componentalpha DNA polymerase:primase complex
G0006260biological_processDNA replication
G0006269biological_processDNA replication, synthesis of primer
G0006270biological_processDNA replication initiation
Functional Information from PROSITE/UniProt
site_idPS00116
Number of Residues9
DetailsDNA_POLYMERASE_B DNA polymerase family B signature. YGDTDSIMI
ChainResidueDetails
FTYR1000-ILE1008
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues98
DetailsDNA binding: {"description":"OB"}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues104
DetailsRegion: {"description":"Winged helix-turn-helix (wHTH) 1"}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues72
DetailsRegion: {"description":"Winged helix-turn-helix (wHTH) 2"}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues19
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI5
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_FI6
Number of Residues10
DetailsCompositional bias: {"description":"Acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues3
DetailsActive site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24043831","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31479243","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"31479243","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6R4S","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
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_FI11
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_FI12
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"31479243","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues142
DetailsRegion: {"description":"RNA:DNA duplex-binding","evidences":[{"source":"PubMed","id":"26975377","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI14
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_FI15
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17893144","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25550159","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues35
DetailsZinc finger: {"description":"CysA-type","evidences":[{"source":"UniProtKB","id":"P15436","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues65
DetailsRegion: {"description":"DNA-binding","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues26
DetailsMotif: {"description":"CysB motif","evidences":[{"source":"UniProtKB","id":"P15436","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"26975377","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5EXR","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P33609","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"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_FI24
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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