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8FOC

Cryo-EM structure of S. cerevisiae DNA polymerase alpha-primase in Apo state conformation I

Functional Information from GO Data
ChainGOidnamespacecontents
10000166molecular_functionnucleotide binding
10000510molecular_functionH3-H4 histone complex chaperone activity
10000731biological_processDNA synthesis involved in DNA repair
10003676molecular_functionnucleic acid binding
10003677molecular_functionDNA binding
10003682molecular_functionchromatin binding
10003688molecular_functionDNA replication origin binding
10003697molecular_functionsingle-stranded DNA binding
10003887molecular_functionDNA-directed DNA polymerase activity
10005515molecular_functionprotein binding
10005634cellular_componentnucleus
10005657cellular_componentreplication fork
10005658cellular_componentalpha DNA polymerase:primase complex
10005739cellular_componentmitochondrion
10006260biological_processDNA replication
10006270biological_processDNA replication initiation
10006272biological_processleading strand elongation
10006273biological_processlagging strand elongation
10006278biological_processRNA-templated DNA biosynthetic process
10006279biological_processpremeiotic DNA replication
10006281biological_processDNA repair
10006302biological_processdouble-strand break repair
10008270molecular_functionzinc ion binding
10016740molecular_functiontransferase activity
10016779molecular_functionnucleotidyltransferase activity
10034061molecular_functionDNA polymerase activity
10046872molecular_functionmetal ion binding
10051536molecular_functioniron-sulfur cluster binding
10051539molecular_function4 iron, 4 sulfur cluster binding
11902975biological_processmitotic DNA replication initiation
A0000166molecular_functionnucleotide binding
A0000428cellular_componentDNA-directed RNA polymerase complex
A0003697molecular_functionsingle-stranded DNA binding
A0003899molecular_functionDNA-directed RNA polymerase activity
A0005524molecular_functionATP binding
A0005658cellular_componentalpha DNA polymerase:primase complex
A0006260biological_processDNA replication
A0006269biological_processDNA replication, synthesis of primer
A0006270biological_processDNA replication initiation
A0008270molecular_functionzinc ion binding
A0016740molecular_functiontransferase activity
A0016779molecular_functionnucleotidyltransferase activity
A0043596cellular_componentnuclear replication fork
A0046872molecular_functionmetal ion binding
B0003677molecular_functionDNA binding
B0003697molecular_functionsingle-stranded DNA binding
B0003899molecular_functionDNA-directed RNA polymerase activity
B0005634cellular_componentnucleus
B0005635cellular_componentnuclear envelope
B0005658cellular_componentalpha DNA polymerase:primase complex
B0006260biological_processDNA replication
B0006261biological_processDNA-templated DNA replication
B0006269biological_processDNA replication, synthesis of primer
B0006270biological_processDNA replication initiation
B0006302biological_processdouble-strand break repair
B0046872molecular_functionmetal ion binding
B0051536molecular_functioniron-sulfur cluster binding
B0051539molecular_function4 iron, 4 sulfur cluster binding
C0003677molecular_functionDNA binding
C0003887molecular_functionDNA-directed DNA polymerase activity
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005635cellular_componentnuclear envelope
C0005658cellular_componentalpha DNA polymerase:primase complex
C0006260biological_processDNA replication
C0006270biological_processDNA replication initiation
C0016233biological_processtelomere capping
C0071897biological_processDNA biosynthetic process
Functional Information from PROSITE/UniProt
site_idPS00116
Number of Residues9
DetailsDNA_POLYMERASE_B DNA polymerase family B signature. YGDTDSVMI
ChainResidueDetails
1TYR994-ILE1002

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198
ChainResidueDetails
CSER126
BCYS417
BCYS434
BCYS474

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:19494830, ECO:0007744|PDB:3FLO
ChainResidueDetails
1CYS1287
1CYS1290
1CYS1314
1CYS1317
1CYS1348
1CYS1353
1CYS1367
1CYS1372

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0007744|PubMed:22814378
ChainResidueDetails
1SER2

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
1SER31
1SER240
1SER274

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198
ChainResidueDetails
1SER82
1SER83
1SER84
1SER169

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198
ChainResidueDetails
1SER170

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19779198
ChainResidueDetails
1THR172
1THR309

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198
ChainResidueDetails
1THR313

237992

PDB entries from 2025-06-25

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