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6TTG

Crystal structure of the ATP binding domain of S. aureus GyrB complexed with LMD62

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 Residues14
Detailsbinding site for residue NWK A 301
ChainResidue
AASN54
APRO87
AILE102
AARG144
AHOH411
AHOH428
ASER55
AGLU58
AGLU58
AASP81
AARG84
AARG84
AGLY85
AILE86

site_idAC2
Number of Residues8
Detailsbinding site for residue GOL A 302
ChainResidue
AMET34
AARG200
AGLU201
AHOH415
BILE90
BGLY95
BARG96
BPRO97

site_idAC3
Number of Residues3
Detailsbinding site for residue MPD A 303
ChainResidue
AHIS143
AMPD304
AHOH453

site_idAC4
Number of Residues6
Detailsbinding site for residue MPD A 304
ChainResidue
AASP81
AHIS143
ALYS170
ATHR171
AMPD303
AHOH453

site_idAC5
Number of Residues3
Detailsbinding site for residue MPD A 305
ChainResidue
AGLN66
ATHR80
AHOH446

site_idAC6
Number of Residues6
Detailsbinding site for residue CA A 306
ChainResidue
AASP57
AASP57
AHOH474
AHOH474
AHOH501
AHOH501

site_idAC7
Number of Residues3
Detailsbinding site for residue CL A 307
ChainResidue
AVAL88
AASP89
AARG144

site_idAC8
Number of Residues15
Detailsbinding site for residue NWK B 301
ChainResidue
ATHR185
BASN54
BSER55
BGLU58
BASP81
BARG84
BGLY85
BILE86
BPRO87
BARG144
BTHR173
BILE175
BHOH403
BHOH420
BHOH423

site_idAC9
Number of Residues6
Detailsbinding site for residue MPD B 302
ChainResidue
BHIS143
BGLU186
BTHR187
BVAL189
BMPD303
BHOH439

site_idAD1
Number of Residues4
Detailsbinding site for residue MPD B 303
ChainResidue
BASP81
BHIS143
BLYS170
BMPD302

site_idAD2
Number of Residues1
Detailsbinding site for residue IMD B 304
ChainResidue
BHOH440

site_idAD3
Number of Residues3
Detailsbinding site for residue CL B 305
ChainResidue
BVAL88
BASP89
BARG144

Functional Information from PROSITE/UniProt
site_idPS00154
Number of Residues7
DetailsATPASE_E1_E2 E1-E2 ATPases phosphorylation site. DKTGTVI
ChainResidueDetails
AASP169-ILE175

246704

PDB entries from 2025-12-24

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