Structure of PDB 6fqv Chain T

Receptor sequence
>6fqvT (length=482) Species: 158879 (Staphylococcus aureus subsp. aureus N315) [Search protein sequence]
NERNITSEMRESFLDYAMSVIVARALPDVRDGLKPVHRRILYGLNEQGMT
PDKSYKKSARIVGDVMGKYHPHGDSSIYEAMVRMAQDFSYRYPLVDGQGN
FGSMDGDGAAAMRYTEARMTKITLELLRDINKDTIDFIDNYDGNEREPSV
LPARFPNLLANGASGIAVGMATNIPPHNLTELINGVLSLSKNPDISIAEL
MEDIEGPDFPTAGLILGKSGIRRAYETGRGSIQMRSRAVIEERGGGRQRI
VVTEIPFQVNKARMIEKIAELVRDKKIDGITDLRDETSLRTGVRVVIDVR
KDANASVILNNLYKQTPLQTSFGVNMIALVNGRPKLINLKEALVHYLEHQ
KTVVRRRTQYNLRKAKDRAHILEGLRIALDHIDEIISTIRESDTDKVAME
SLQQRFKLSEKQAQAILDMRLRRLTGLERDKIEAEYNELLNYISELETIL
ADEEVLLQLVRDELTEIRDRFGDDRRTEIQLG
3D structure
PDB6fqv A new class of antibacterials, the imidazopyrazinones, reveal structural transitions involved in DNA gyrase poisoning and mechanisms of resistance.
ChainT
Resolution2.6 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 T Y25 R122 I175 A176 G178 M179 A180 R238 S330 Y16 R113 I166 A167 G169 M170 A171 R229 S321
BS02 dna T R33 K43 H46 H79 H81 R92 I175 R272 R24 K34 H37 H70 H72 R83 I166 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
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Biological Process
External links
PDB RCSB:6fqv, PDBe:6fqv, PDBj:6fqv
PDBsum6fqv
PubMed29538767
UniProtQ99XG5|GYRA_STAAN DNA gyrase subunit A (Gene Name=gyrA)

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