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5D6P

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 Residues14
Detailsbinding site for residue 57U A 301
ChainResidue
AILE51
APRO87
AILE102
ATHR173
AGOL303
AHOH424
AASN54
ASER55
AGLU58
AVAL79
AASP81
AARG84
AGLY85
AILE86

site_idAC2
Number of Residues5
Detailsbinding site for residue MPD A 302
ChainResidue
ATHR80
AASP81
AHIS143
ATHR171
AGLY172

site_idAC3
Number of Residues5
Detailsbinding site for residue GOL A 303
ChainResidue
AILE51
AASN54
AILE102
ASER129
A57U301

site_idAC4
Number of Residues14
Detailsbinding site for residue 57U B 301
ChainResidue
BILE51
BASN54
BSER55
BGLU58
BVAL79
BASP81
BARG84
BGLY85
BILE86
BPRO87
BILE102
BILE175
BHOH414
BHOH454

site_idAC5
Number of Residues3
Detailsbinding site for residue MPD B 302
ChainResidue
BHIS143
BLYS170
BMPD303

site_idAC6
Number of Residues4
Detailsbinding site for residue MPD B 303
ChainResidue
BHIS143
BGLU186
BVAL189
BMPD302

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

237992

PDB entries from 2025-06-25

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