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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

5IKN

Crystal Structure of the T7 Replisome in the Absence of DNA

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003676molecular_functionnucleic acid binding
A0003677molecular_functionDNA binding
A0003824molecular_functioncatalytic activity
A0003887molecular_functionDNA-directed DNA polymerase activity
A0004518molecular_functionnuclease activity
A0004527molecular_functionexonuclease activity
A0004529molecular_functionDNA exonuclease activity
A0005515molecular_functionprotein binding
A0006259biological_processDNA metabolic process
A0006260biological_processDNA replication
A0006261biological_processDNA-templated DNA replication
A0006302biological_processdouble-strand break repair
A0008408molecular_function3'-5' exonuclease activity
A0016740molecular_functiontransferase activity
A0016779molecular_functionnucleotidyltransferase activity
A0016787molecular_functionhydrolase activity
A0034061molecular_functionDNA polymerase activity
A0039693biological_processviral DNA genome replication
A0046872molecular_functionmetal ion binding
A0090592biological_processDNA synthesis involved in DNA replication
B0000166molecular_functionnucleotide binding
B0003676molecular_functionnucleic acid binding
B0003677molecular_functionDNA binding
B0003824molecular_functioncatalytic activity
B0003887molecular_functionDNA-directed DNA polymerase activity
B0004518molecular_functionnuclease activity
B0004527molecular_functionexonuclease activity
B0004529molecular_functionDNA exonuclease activity
B0005515molecular_functionprotein binding
B0006259biological_processDNA metabolic process
B0006260biological_processDNA replication
B0006261biological_processDNA-templated DNA replication
B0006302biological_processdouble-strand break repair
B0008408molecular_function3'-5' exonuclease activity
B0016740molecular_functiontransferase activity
B0016779molecular_functionnucleotidyltransferase activity
B0016787molecular_functionhydrolase activity
B0034061molecular_functionDNA polymerase activity
B0039693biological_processviral DNA genome replication
B0046872molecular_functionmetal ion binding
B0090592biological_processDNA synthesis involved in DNA replication
C0000166molecular_functionnucleotide binding
C0003676molecular_functionnucleic acid binding
C0003677molecular_functionDNA binding
C0003824molecular_functioncatalytic activity
C0003887molecular_functionDNA-directed DNA polymerase activity
C0004518molecular_functionnuclease activity
C0004527molecular_functionexonuclease activity
C0004529molecular_functionDNA exonuclease activity
C0005515molecular_functionprotein binding
C0006259biological_processDNA metabolic process
C0006260biological_processDNA replication
C0006261biological_processDNA-templated DNA replication
C0006302biological_processdouble-strand break repair
C0008408molecular_function3'-5' exonuclease activity
C0016740molecular_functiontransferase activity
C0016779molecular_functionnucleotidyltransferase activity
C0016787molecular_functionhydrolase activity
C0034061molecular_functionDNA polymerase activity
C0039693biological_processviral DNA genome replication
C0046872molecular_functionmetal ion binding
C0090592biological_processDNA synthesis involved in DNA replication
D0003678molecular_functionDNA helicase activity
D0003697molecular_functionsingle-stranded DNA binding
D0005524molecular_functionATP binding
D0006260biological_processDNA replication
D0043139molecular_function5'-3' DNA helicase activity
E0003678molecular_functionDNA helicase activity
E0003697molecular_functionsingle-stranded DNA binding
E0005524molecular_functionATP binding
E0006260biological_processDNA replication
E0043139molecular_function5'-3' DNA helicase activity
F0003678molecular_functionDNA helicase activity
F0003697molecular_functionsingle-stranded DNA binding
F0005524molecular_functionATP binding
F0006260biological_processDNA replication
F0043139molecular_function5'-3' DNA helicase activity
G0003678molecular_functionDNA helicase activity
G0003697molecular_functionsingle-stranded DNA binding
G0005524molecular_functionATP binding
G0006260biological_processDNA replication
G0043139molecular_function5'-3' DNA helicase activity
H0003678molecular_functionDNA helicase activity
H0003697molecular_functionsingle-stranded DNA binding
H0005524molecular_functionATP binding
H0006260biological_processDNA replication
H0043139molecular_function5'-3' DNA helicase activity
I0003678molecular_functionDNA helicase activity
I0003697molecular_functionsingle-stranded DNA binding
I0005524molecular_functionATP binding
I0006260biological_processDNA replication
I0043139molecular_function5'-3' DNA helicase activity
J0003678molecular_functionDNA helicase activity
J0003697molecular_functionsingle-stranded DNA binding
J0005524molecular_functionATP binding
J0006260biological_processDNA replication
J0043139molecular_function5'-3' DNA helicase activity
K0005737cellular_componentcytoplasm
K0005829cellular_componentcytosol
K0015035molecular_functionprotein-disulfide reductase activity
K0045454biological_processcell redox homeostasis
L0005737cellular_componentcytoplasm
L0005829cellular_componentcytosol
L0015035molecular_functionprotein-disulfide reductase activity
L0045454biological_processcell redox homeostasis
M0005737cellular_componentcytoplasm
M0005829cellular_componentcytosol
M0015035molecular_functionprotein-disulfide reductase activity
M0045454biological_processcell redox homeostasis
Functional Information from PROSITE/UniProt
site_idPS00194
Number of Residues19
DetailsTHIOREDOXIN_1 Thioredoxin family active site. LVdFWaeWCGPCKmIapiL
ChainResidueDetails
KLEU24-LEU42
site_idPS00447
Number of Residues20
DetailsDNA_POLYMERASE_A DNA polymerase family A signature. RdnAKtfiYGflYgaGdekI
ChainResidueDetails
AARG518-ILE537
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues558
DetailsRegion: {"description":"3'-5'exonuclease","evidences":[{"source":"HAMAP-Rule","id":"MF_04101","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"9440688","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_04101","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"9440688","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_04101","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"9440688","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9914251","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_04101","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"9914251","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues609
DetailsDomain: {"description":"Toprim","evidences":[{"source":"PROSITE-ProRule","id":"PRU00995","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1068
DetailsDomain: {"description":"SF4 helicase","evidences":[{"source":"HAMAP-Rule","id":"MF_04154","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_04154","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12769857","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_04154","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12769857","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues49
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_04154","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues7
DetailsSite: {"description":"dTTP/dATP binding","evidences":[{"source":"HAMAP-Rule","id":"MF_04154","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10892646","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues7
DetailsSite: {"description":"dTTP/dATP binding","evidences":[{"source":"HAMAP-Rule","id":"MF_04154","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10535735","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues21
DetailsSite: {"description":"dTTP/dATP binding","evidences":[{"source":"HAMAP-Rule","id":"MF_04154","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10535735","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"10892646","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues6
DetailsActive site: {"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues3
DetailsSite: {"description":"Deprotonates C-terminal active site Cys","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues6
DetailsSite: {"description":"Contributes to redox potential value","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues3
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

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PDB entries from 2025-08-27

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