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4DDX

Thermotoga maritima reverse gyrase, primitive monoclinic form

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003676molecular_functionnucleic acid binding
A0003677molecular_functionDNA binding
A0003916molecular_functionDNA topoisomerase activity
A0003918molecular_functionDNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006260biological_processDNA replication
A0006265biological_processDNA topological change
A0008094molecular_functionATP-dependent activity, acting on DNA
A0008270molecular_functionzinc ion binding
A0016853molecular_functionisomerase activity
A0016887molecular_functionATP hydrolysis activity
A0046872molecular_functionmetal ion binding
A0160097molecular_functionreverse gyrase activity
B0000166molecular_functionnucleotide binding
B0003676molecular_functionnucleic acid binding
B0003677molecular_functionDNA binding
B0003916molecular_functionDNA topoisomerase activity
B0003918molecular_functionDNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006260biological_processDNA replication
B0006265biological_processDNA topological change
B0008094molecular_functionATP-dependent activity, acting on DNA
B0008270molecular_functionzinc ion binding
B0016853molecular_functionisomerase activity
B0016887molecular_functionATP hydrolysis activity
B0046872molecular_functionmetal ion binding
B0160097molecular_functionreverse gyrase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1201
ChainResidue
ACYS621
ACYS624
ACYS635
ACYS638

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1202
ChainResidue
ACYS11
ACYS14
ACYS29
ACYS32

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1201
ChainResidue
BCYS624
BCYS635
BCYS638
BCYS621

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1202
ChainResidue
BCYS11
BCYS14
BCYS29
BCYS32

Functional Information from PROSITE/UniProt
site_idPS00572
Number of Residues9
DetailsGLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. LLVLENGVN
ChainResidueDetails
ALEU778-ASN786

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues310
DetailsDomain: {"description":"Helicase ATP-binding","evidences":[{"source":"HAMAP-Rule","id":"MF_01125","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues444
DetailsDomain: {"description":"Helicase C-terminal","evidences":[{"source":"HAMAP-Rule","id":"MF_01125","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues314
DetailsDomain: {"description":"Toprim","evidences":[{"source":"HAMAP-Rule","id":"MF_01125","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues772
DetailsDomain: {"description":"Topo IA-type catalytic","evidences":[{"source":"PROSITE-ProRule","id":"PRU01383","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues54
DetailsZinc finger: {"description":"RG C-terminal-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU01381","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23209025","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues54
DetailsRegion: {"description":"Insert region","evidences":[{"source":"PubMed","id":"23209025","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues140
DetailsRegion: {"description":"Latch region","evidences":[{"source":"PubMed","id":"21051354","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21627332","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23209025","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues6
DetailsMotif: {"description":"DEAD box","evidences":[{"source":"HAMAP-Rule","id":"MF_01125","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsActive site: {"description":"O-(5'-phospho-DNA)-tyrosine intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18614530","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01125","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23209025","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7FSE","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"7FSF","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"8OFB","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"4DDT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4DDU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4DDV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4DDW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4DDX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21627332","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3P4X","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01125","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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