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5CPH

Crystal structure of the ATP binding domain of S. aureus GyrB complexed with a 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 Residues8
Detailsbinding site for residue EVO A 301
ChainResidue
AASN54
AGLU58
AASP81
AILE86
AILE102
AILE175
AHOH427
AHOH446

site_idAC2
Number of Residues8
Detailsbinding site for residue SO4 A 302
ChainResidue
AASP81
AHIS143
ALYS170
ATHR171
AGLY172
AHOH443
AHOH499
ATHR80

site_idAC3
Number of Residues7
Detailsbinding site for residue MPD B 301
ChainResidue
BHIS143
BVAL174
BGLU186
BTHR187
BHOH479
BHOH535
BHOH579

site_idAC4
Number of Residues7
Detailsbinding site for residue EVO B 302
ChainResidue
BASN54
BGLU58
BASP81
BILE86
BILE102
BHOH455
BHOH586

site_idAC5
Number of Residues9
Detailsbinding site for residue SO4 B 303
ChainResidue
BTHR80
BASP81
BHIS143
BLYS170
BTHR171
BGLY172
BTHR173
BHOH410
BHOH479

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

238895

PDB entries from 2025-07-16

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