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4DUH

Crystal structure of 24 kDa domain of E. coli DNA gyrase B in complex with small molecule inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003918molecular_functionDNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
A0005524molecular_functionATP binding
A0006265biological_processDNA topological change
B0003677molecular_functionDNA binding
B0003918molecular_functionDNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
B0005524molecular_functionATP binding
B0006265biological_processDNA topological change
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE RLI A 301
ChainResidue
AVAL43
AARG136
ATHR165
AHOH614
AHOH702
AASN46
AGLU50
AASP73
AARG76
AILE78
APRO79
AGLY101
ALYS103

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE RLI B 301
ChainResidue
BVAL43
BASN46
BGLU50
BVAL71
BASP73
BARG76
BILE78
BPRO79
BILE94
BGLY101
BARG136
BTHR165
BHOH451

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor (ATPase activity)","evidences":[{"source":"PubMed","id":"10734094","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"8248233","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10734094","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25202966","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25849408","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues13
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25849408","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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