Structure of PDB 5cdq Chain R

Receptor sequence
>5cdqR (length=481) Species: 158879 (Staphylococcus aureus subsp. aureus N315) [Search protein sequence]
NERNITSEMRESFLDYAMSVIVARALPDVRDGLKPVHRRILYGLNEQGMT
PDKSYKKSARIVGDVMGKYHPHGDSSIYEAMVRMAQDFSYRYPLVDGQGN
FGSMDGDGAAAMRYTEARMTKITLELLRDINKDTIDFIDNYDGNEREPSV
LPARFPNLLANGASGIAVGMATNIPPHNLTELINGVLSLSKNPDISIAEL
MEDIEGPDFPTAGLILGKSGIRRAYETGRGSIQMRSRAVIEERGGGRQRI
VVTEIPFQVNKARMIEKIAELVRDKKIDGITDLRDETSLRTGVRVVIDVR
KDANASVILNNLYKQTPLQTSFGVNMIALVNGRPKLINLKEALVHYLEHQ
KTVVRRRTQYNLRKAKDRAHILEGLRIALDHIDEIISTIRESDTDKVAME
SLQQRFKLSEKQAQAILDMRLRRLTGLERDKIEAEYNELLNYISELETIL
ADEEVLLQLVRDELTEIRDRFGDDRRTEIQL
3D structure
PDB5cdq Structural basis of DNA gyrase inhibition by antibacterial QPT-1, anticancer drug etoposide and moxifloxacin.
ChainR
Resolution2.95 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 5.6.2.2: DNA topoisomerase (ATP-hydrolyzing).
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 dna R Y123 I175 G178 M179 Y114 I166 G169 M170
BS02 dna R R33 K43 H46 H79 H81 S85 R92 R272 R24 K34 H37 H70 H72 S76 R83 R263
Gene Ontology
Molecular Function
GO:0003677 DNA binding
GO:0003918 DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
GO:0005524 ATP binding
Biological Process
GO:0006259 DNA metabolic process
GO:0006265 DNA topological change

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5cdq, PDBe:5cdq, PDBj:5cdq
PDBsum5cdq
PubMed26640131
UniProtQ99XG5|GYRA_STAAN DNA gyrase subunit A (Gene Name=gyrA)

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