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5CTX

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 Residues6
Detailsbinding site for residue MPD A 301
ChainResidue
AASP81
AHIS143
ALYS170
ATHR171
AMPD302
AHOH404

site_idAC2
Number of Residues3
Detailsbinding site for residue MPD A 302
ChainResidue
ATYR141
AHIS143
AMPD301

site_idAC3
Number of Residues6
Detailsbinding site for residue MPD B 301
ChainResidue
BTHR80
BASP81
BHIS143
BLYS170
BMPD302
BHOH414

site_idAC4
Number of Residues4
Detailsbinding site for residue MPD B 302
ChainResidue
BTYR141
BHIS143
BGLU186
BMPD301

site_idAC5
Number of Residues13
Detailsbinding site for residue 55G B 303
ChainResidue
ATHR185
BASN54
BGLU58
BASP81
BARG84
BGLY85
BPRO87
BILE102
BARG144
BILE175
BHOH424
BHOH449
BHOH467

site_idAC6
Number of Residues6
Detailsbinding site for residue MG B 304
ChainResidue
AHOH484
BASP53
BASP57
BHOH419
BHOH429
BHOH451

site_idAC7
Number of Residues5
Detailsbinding site for residue MG B 305
ChainResidue
BGLU164
BGLU219
BHOH468
BHOH528
BHOH530

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

226707

PDB entries from 2024-10-30

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