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7DQI

E. coli GyrB ATPase domain in complex with Esculetin

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 Residues9
Detailsbinding site for residue HFC A 302
ChainResidue
AASP73
AILE78
AVAL120
ATHR165
AVAL167
AVAL43
AASN46
AALA47
AVAL71

site_idAC3
Number of Residues10
Detailsbinding site for residue HFC B 301
ChainResidue
BVAL43
BASN46
BALA47
BVAL71
BASP73
BILE78
BILE94
BVAL120
BTHR165
BVAL167

site_idAC4
Number of Residues5
Detailsbinding site for residue PO4 B 302
ChainResidue
BALA65
BASP66
BPO4303
BHOH405
BHOH426

site_idAC5
Number of Residues6
Detailsbinding site for residue PO4 B 303
ChainResidue
BHIS55
BHIS64
BARG168
BLYS208
BPO4302
BHOH405

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 2024-07-24

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