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4NL8

PriA Helicase Bound to SSB C-terminal Tail Peptide

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003676molecular_functionnucleic acid binding
A0003677molecular_functionDNA binding
A0003678molecular_functionDNA helicase activity
A0004386molecular_functionhelicase activity
A0005524molecular_functionATP binding
A0006260biological_processDNA replication
A0006269biological_processDNA replication, synthesis of primer
A0006270biological_processDNA replication initiation
A0006302biological_processdouble-strand break repair
A0006310biological_processDNA recombination
A0008270molecular_functionzinc ion binding
A0016787molecular_functionhydrolase activity
A0016853molecular_functionisomerase activity
A0016887molecular_functionATP hydrolysis activity
A0043138molecular_function3'-5' DNA helicase activity
A0046872molecular_functionmetal ion binding
A1990077cellular_componentprimosome complex
B0000166molecular_functionnucleotide binding
B0003676molecular_functionnucleic acid binding
B0003677molecular_functionDNA binding
B0003678molecular_functionDNA helicase activity
B0004386molecular_functionhelicase activity
B0005524molecular_functionATP binding
B0006260biological_processDNA replication
B0006269biological_processDNA replication, synthesis of primer
B0006270biological_processDNA replication initiation
B0006302biological_processdouble-strand break repair
B0006310biological_processDNA recombination
B0008270molecular_functionzinc ion binding
B0016787molecular_functionhydrolase activity
B0016853molecular_functionisomerase activity
B0016887molecular_functionATP hydrolysis activity
B0043138molecular_function3'-5' DNA helicase activity
B0046872molecular_functionmetal ion binding
B1990077cellular_componentprimosome complex
E0000166molecular_functionnucleotide binding
E0003676molecular_functionnucleic acid binding
E0003677molecular_functionDNA binding
E0003678molecular_functionDNA helicase activity
E0004386molecular_functionhelicase activity
E0005524molecular_functionATP binding
E0006260biological_processDNA replication
E0006269biological_processDNA replication, synthesis of primer
E0006270biological_processDNA replication initiation
E0006302biological_processdouble-strand break repair
E0006310biological_processDNA recombination
E0008270molecular_functionzinc ion binding
E0016787molecular_functionhydrolase activity
E0016853molecular_functionisomerase activity
E0016887molecular_functionATP hydrolysis activity
E0043138molecular_function3'-5' DNA helicase activity
E0046872molecular_functionmetal ion binding
E1990077cellular_componentprimosome complex
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 801
ChainResidue
ACYS435
ACYS438
ACYS475
ACYS478

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 802
ChainResidue
ACYS444
ACYS447
ACYS462
ACYS465

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 801
ChainResidue
BCYS438
BCYS475
BCYS478
BCYS435

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 802
ChainResidue
BCYS444
BCYS447
BCYS462
BCYS465

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN E 801
ChainResidue
ECYS444
ECYS447
ECYS462
ECYS465

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN E 802
ChainResidue
ECYS435
ECYS438
ECYS475
ECYS478

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues498
DetailsDomain: {"description":"Helicase ATP-binding","evidences":[{"source":"HAMAP-Rule","id":"MF_00983","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues525
DetailsRegion: {"description":"Helicase lobe 1","evidences":[{"source":"PubMed","id":"24379377","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues129
DetailsRegion: {"description":"Helicase lobe 2, N-terminus","evidences":[{"source":"PubMed","id":"24379377","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues162
DetailsRegion: {"description":"CRR","evidences":[{"source":"PubMed","id":"24379377","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues9
DetailsMotif: {"description":"DEAH box","evidences":[{"source":"HAMAP-Rule","id":"MF_00983","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues42
DetailsMotif: {"description":"Aromatic-rich loop (ARL)","evidences":[{"source":"PubMed","id":"24379377","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues21
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00983","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"PDB","id":"4NL4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00983","evidenceCode":"ECO:0000255"},{"source":"PDB","id":"4NL4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4NL8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6DGD","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24379377","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4NL4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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