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5D6Q

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

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 Residues6
Detailsbinding site for residue MPD A 301
ChainResidue
AASP81
AHIS143
ALYS170
ATHR171
AMPD302
AHOH412

site_idAC2
Number of Residues2
Detailsbinding site for residue MPD A 302
ChainResidue
AHIS143
AMPD301

site_idAC3
Number of Residues6
Detailsbinding site for residue MPD B 301
ChainResidue
BASP81
BHIS143
BLYS170
BGLY172
BMPD302
BTHR80

site_idAC4
Number of Residues5
Detailsbinding site for residue MPD B 302
ChainResidue
BHIS143
BVAL174
BGLU186
BMPD301
BHOH405

site_idAC5
Number of Residues15
Detailsbinding site for residue 57V B 303
ChainResidue
ATHR185
BASN54
BSER55
BVAL79
BASP81
BARG84
BGLY85
BILE86
BPRO87
BILE102
BARG144
BTHR173
BHOH414
BHOH438
BHOH490

site_idAC6
Number of Residues5
Detailsbinding site for residue MG B 304
ChainResidue
BGLU164
BGLU219
BHOH421
BHOH525
BHOH530

site_idAC7
Number of Residues5
Detailsbinding site for residue MG B 305
ChainResidue
BASN82
BGLY83
BTHR171
BHOH443
BHOH536

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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