Structure of PDB 6fqv Chain C

Receptor sequence
>6fqvC (length=473) Species: 158879 (Staphylococcus aureus subsp. aureus N315) [Search protein sequence]
NERNITSEMRESFLDYAMSVIVARALPDVRDGLKPVHRRILYGLNEQGMT
PDKSYKKSARIVGDVMGKYHPHGDSSIYEAMVRMAQDFSYRYPLVDGQGN
FGSMDGDGAAAMRYTEARMTKITLELLRDINKDTIDFIDNYDGNEREPSV
LPARFPNLLANGASGIAVGMATNIPPHNLTELINGVLSLSKNPDISIAEL
MEDIEGPDFPTAGLILGKSGIRRAYETGRGSIQMRSRAVRIVVTEIPFQV
NKARMIEKIAELVRDKKIDGITDLRDETSLRTGVRVVIDVRKDANASVIL
NNLYKQTPLQTSFGVNMIALVNGRPKLINLKEALVHYLEHQKTVVRRRTQ
YNLRKAKDRAHILEGLRIALDHIDEIISTIRESDTDKVAMESLQQRFKLS
EKQAQAILDMRLRRLTGLERDKIEAEYNELLNYISELETILADEEVLLQL
VRDELTEIRDRFGDDRRTEIQLG
3D structure
PDB6fqv A new class of antibacterials, the imidazopyrazinones, reveal structural transitions involved in DNA gyrase poisoning and mechanisms of resistance.
ChainC
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 C Y25 R122 Y123 I175 A176 G178 M179 R238 Y16 R113 Y114 I166 A167 G169 M170 R229
BS02 dna C R33 K43 H46 H79 H81 R92 I175 R24 K34 H37 H70 H72 R83 I166
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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