Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7OPL

CryoEM structure of DNA Polymerase alpha - primase bound to SARS CoV nsp1

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003676molecular_functionnucleic acid binding
A0003677molecular_functionDNA binding
A0003887molecular_functionDNA-directed DNA polymerase activity
A0006260biological_processDNA replication
A1902975biological_processmitotic DNA replication initiation
B0003677molecular_functionDNA binding
B0006260biological_processDNA replication
C0000287molecular_functionmagnesium ion binding
C0000428cellular_componentDNA-directed RNA polymerase complex
C0003896molecular_functionDNA primase activity
C0005515molecular_functionprotein binding
C0005654cellular_componentnucleoplasm
C0005658cellular_componentalpha DNA polymerase:primase complex
C0006260biological_processDNA replication
C0006269biological_processDNA replication, synthesis of primer
C0006270biological_processDNA replication initiation
C0008270molecular_functionzinc ion binding
C0016020cellular_componentmembrane
C0016779molecular_functionnucleotidyltransferase activity
C0032553molecular_functionribonucleotide binding
C0046872molecular_functionmetal ion binding
C1990077cellular_componentprimosome complex
D0003677molecular_functionDNA binding
D0005515molecular_functionprotein binding
D0005654cellular_componentnucleoplasm
D0005658cellular_componentalpha DNA polymerase:primase complex
D0006260biological_processDNA replication
D0006261biological_processDNA-templated DNA replication
D0006269biological_processDNA replication, synthesis of primer
D0006270biological_processDNA replication initiation
D0046872molecular_functionmetal ion binding
D0051539molecular_function4 iron, 4 sulfur cluster binding
D0071667molecular_functionDNA/RNA hybrid binding
D1903934biological_processpositive regulation of DNA primase activity
D1990077cellular_componentprimosome complex
Functional Information from PROSITE/UniProt
site_idPS00116
Number of Residues9
DetailsDNA_POLYMERASE_B DNA polymerase family B signature. YGDTDSIMI
ChainResidueDetails
ATYR1000-ILE1008

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:17893144, ECO:0000269|PubMed:25550159, ECO:0000269|PubMed:26975377
ChainResidueDetails
DCYS287
DCYS367
DCYS424

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:17893144, ECO:0000269|PubMed:25550159
ChainResidueDetails
DCYS384
CASP111
CASP306
ACYS1315
ACYS1348
ACYS1353
ACYS1371
ACYS1374

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
DTHR470
CCYS122
CCYS128
CCYS131

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:24043831, ECO:0000269|PubMed:24239947, ECO:0000269|PubMed:31479243
ChainResidueDetails
CSER160

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:24043831, ECO:0000269|PubMed:31479243
ChainResidueDetails
CHIS315

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:31479243
ChainResidueDetails
CHIS324

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22223895
ChainResidueDetails
CMET1

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon