Structure of PDB 5cdp Chain A

Receptor sequence
>5cdpA (length=483) Species: 158879 (Staphylococcus aureus subsp. aureus N315) [Search protein sequence]
INERNITSEMRESFLDYAMSVIVARALPDVRDGLKPVHRRILYGLNEQGM
TPDKSYKKSARIVGDVMGKYHPHGDSSIYEAMVRMAQDFSYRYPLVDGQG
NFGSMDGDGAAAMRFTEARMTKITLELLRDINKDTIDFIDNYDGNEREPS
VLPARFPNLLANGASGIAVGMATNIPPHNLTELINGVLSLSKNPDISIAE
LMEDIEGPDFPTAGLILGKSGIRRAYETGRGSIQMRSRAVIEERGGGRQR
IVVTEIPFQVNKARMIEKIAELVRDKKIDGITDLRDETSLRTGVRVVIDV
RKDANASVILNNLYKQTPLQTSFGVNMIALVNGRPKLINLKEALVHYLEH
QKTVVRRRTQYNLRKAKDRAHILEGLRIALDHIDEIISTIRESDTDKVAM
ESLQQRFKLSEKQAQAILDMRLRRLTGLERDKIEAEYNELLNYISELETI
LADEEVLLQLVRDELTEIRDRFGDDRRTEIQLG
3D structure
PDB5cdp Structural basis of DNA gyrase inhibition by antibacterial QPT-1, anticancer drug etoposide and moxifloxacin.
ChainA
Resolution2.45 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 A R33 K43 H46 H79 H81 S85 R92 S173 I175 R272 R25 K35 H38 H71 H73 S77 R84 S165 I167 R264
BS02 dna A R122 F123 I175 G178 M179 R238 R114 F115 I167 G170 M171 R230
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:5cdp, PDBe:5cdp, PDBj:5cdp
PDBsum5cdp
PubMed26640131
UniProtQ99XG5|GYRA_STAAN DNA gyrase subunit A (Gene Name=gyrA)

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