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7DQM

E. coli GyrB ATPase domain in complex with Naringenin

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 Residues5
Detailsbinding site for residue AX7 A 301
ChainResidue
AHIS147
AGLU174
BARG20
BHIS147
BGLU174

site_idAC2
Number of Residues4
Detailsbinding site for residue PO4 A 302
ChainResidue
AHIS64
AARG168
ALYS208
AHOH450

site_idAC3
Number of Residues10
Detailsbinding site for residue CWE B 301
ChainResidue
BVAL43
BASN46
BGLU50
BASP73
BILE78
BPRO79
BILE94
BVAL167
BHOH407
BHOH450

site_idAC4
Number of Residues6
Detailsbinding site for residue PO4 B 302
ChainResidue
BHIS55
BHIS64
BARG168
BLYS208
BHOH425
BHOH476

site_idAC5
Number of Residues2
Detailsbinding site for residue PO4 B 303
ChainResidue
BARG204
BHIS215

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor (ATPase activity) => ECO:0000305|PubMed:10734094, ECO:0000305|PubMed:8248233
ChainResidueDetails
AGLU42
BGLU42

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:10734094, ECO:0000269|PubMed:25202966, ECO:0000269|PubMed:25849408
ChainResidueDetails
AASN46
BLEU115
AASP73
AGLY102
ATYR109
ALEU115
BASN46
BASP73
BGLY102
BTYR109

site_idSWS_FT_FI3
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:25849408
ChainResidueDetails
AILE94
BALA100
BLYS103
BASP105
BGLY117
BSER121
AVAL97
AALA100
ALYS103
AASP105
AGLY117
ASER121
BILE94
BVAL97

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PDB entries from 2024-07-10

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