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5Z9E

Bacterial GyrB ATPase domain in complex with a chemical fragment

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 PO4 A 301
ChainResidue
AARG20
ALYS21
APRO23
AHOH420
BGLN151

site_idAC2
Number of Residues5
Detailsbinding site for residue PO4 A 302
ChainResidue
AHOH442
AHIS64
AARG168
ALYS208
AHOH429

site_idAC3
Number of Residues5
Detailsbinding site for residue PO4 A 303
ChainResidue
APRO150
AGLN151
BARG20
BLYS21
BPRO23

site_idAC4
Number of Residues9
Detailsbinding site for residue 27K A 304
ChainResidue
AVAL43
AASN46
AGLU50
AILE78
APRO79
AILE94
AVAL120
AVAL167
AHOH401

site_idAC5
Number of Residues5
Detailsbinding site for residue PO4 B 301
ChainResidue
BHIS55
BHIS64
BARG168
BLYS208
BHOH406

site_idAC6
Number of Residues7
Detailsbinding site for residue 27K B 302
ChainResidue
BVAL43
BASN46
BGLU50
BILE78
BILE94
BVAL167
BHOH401

site_idAC7
Number of Residues4
Detailsbinding site for residue AX7 B 303
ChainResidue
AHIS147
AGLU174
BHIS147
BGLU174

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

219140

PDB entries from 2024-05-01

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