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5D7D

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
AHOH413

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

site_idAC3
Number of Residues4
Detailsbinding site for residue CL A 303
ChainResidue
AVAL88
AARG144
AASN145
AHOH523

site_idAC4
Number of Residues7
Detailsbinding site for residue MG A 304
ChainResidue
AASP57
AASP57
AMG305
AHOH446
AHOH446
AHOH516
AHOH516

site_idAC5
Number of Residues9
Detailsbinding site for residue MG A 305
ChainResidue
AASP53
AASN54
AASP57
AMG304
AMG306
AHOH446
AHOH469
AHOH499
AHOH531

site_idAC6
Number of Residues6
Detailsbinding site for residue MG A 306
ChainResidue
AGLU50
AMG305
AHOH469
AHOH499
AHOH521
AHOH531

site_idAC7
Number of Residues13
Detailsbinding site for residue 57X A 307
ChainResidue
AASN54
ASER55
AGLU58
AVAL79
AASP81
AARG84
AGLY85
AILE86
APRO87
AARG144
ATHR173
AILE175
AHOH442

site_idAC8
Number of Residues5
Detailsbinding site for residue MG A 300
ChainResidue
ALYS163
AHOH450
AHOH475
BASP53
BASP57

site_idAC9
Number of Residues5
Detailsbinding site for residue MPD B 302
ChainResidue
BTHR80
BASP81
BLYS170
BMPD303
BHOH416

site_idAD1
Number of Residues5
Detailsbinding site for residue MPD B 303
ChainResidue
BHIS143
BVAL174
BGLU186
BMPD302
BHOH486

site_idAD2
Number of Residues5
Detailsbinding site for residue CL B 304
ChainResidue
BVAL88
BASP89
BARG144
BASN145
BHOH455

site_idAD3
Number of Residues6
Detailsbinding site for residue MG B 305
ChainResidue
BASN54
BHOH408
BHOH449
BHOH492
BHOH493
BHOH540

site_idAD4
Number of Residues7
Detailsbinding site for residue MG B 306
ChainResidue
BASN82
BGLY83
BTHR171
BHOH467
BHOH479
BHOH508
BHOH510

site_idAD5
Number of Residues6
Detailsbinding site for residue MG B 307
ChainResidue
BGLY208
BHIS228
BHOH462
BHOH483
BHOH521
BHOH524

site_idAD6
Number of Residues15
Detailsbinding site for residue 57X B 308
ChainResidue
BILE175
BHOH435
BHOH502
ATHR185
BASN54
BSER55
BGLU58
BVAL79
BASP81
BARG84
BGLY85
BILE86
BPRO87
BARG144
BTHR173

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

223532

PDB entries from 2024-08-07

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