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6TCK

Crystal structure of the ATP binding domain of S. aureus GyrB complexed with ULD-2

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 N1N A 301
ChainResidue
AASN54
AALA98
AARG144
AHOH407
AHOH420
AHOH428
ASER55
AGLU58
AASP81
AARG84
AARG84
AGLY85
AILE86
APRO87

site_idAC2
Number of Residues6
Detailsbinding site for residue GOL A 302
ChainResidue
AARG200
APHE204
AHOH406
AHOH427
BGLY95
BARG96

site_idAC3
Number of Residues6
Detailsbinding site for residue MPD A 303
ChainResidue
ATHR80
AASP81
AHIS143
ALYS170
AMPD304
AHOH445

site_idAC4
Number of Residues3
Detailsbinding site for residue MPD A 304
ChainResidue
ATYR141
AHIS143
AMPD303

site_idAC5
Number of Residues2
Detailsbinding site for residue MPD A 305
ChainResidue
AGLN66
ATHR80

site_idAC6
Number of Residues4
Detailsbinding site for residue CL A 306
ChainResidue
AVAL88
AASP89
AARG144
AASN145

site_idAC7
Number of Residues18
Detailsbinding site for residue N1N B 301
ChainResidue
ATHR185
AGLU186
AHOH409
BASN54
BSER55
BGLU58
BASP81
BARG84
BGLY85
BILE86
BPRO87
BARG144
BTHR173
BILE175
BHOH411
BHOH427
BHOH440
BHOH484

site_idAC8
Number of Residues7
Detailsbinding site for residue MPD B 302
ChainResidue
BTHR80
BASP81
BHIS143
BLYS170
BTHR171
BMPD303
BHOH441

site_idAC9
Number of Residues6
Detailsbinding site for residue MPD B 303
ChainResidue
BHIS143
BGLU186
BTHR187
BVAL189
BMPD302
BHOH441

site_idAD1
Number of Residues3
Detailsbinding site for residue IMD B 304
ChainResidue
BLEU162
BHOH426
BHOH438

site_idAD2
Number of Residues3
Detailsbinding site for residue CL B 305
ChainResidue
BVAL88
BASP89
BARG144

site_idAD3
Number of Residues4
Detailsbinding site for residue CA B 306
ChainResidue
AGLU224
AHOH413
BGLU224
BHOH432

site_idAD4
Number of Residues5
Detailsbinding site for residue DMS B 307
ChainResidue
BASP74
BASN75
BGLY166
BTHR167
BTHR188

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

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PDB entries from 2024-10-16

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