Structure of PDB 5btc Chain A

Receptor sequence
>5btcA (length=487) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
IEPVDIEQEMQRSYIDYAMSVIVGRALPEVRDGLKPVHRRVLYAMFDSGF
RPDRSHAKSARSVAETMGNYHPHGDSSIYDSLVRMAQPWSLRYPLVDGQG
NFGSPGNDPPAAMRYTEARLTPLAMEMLREIDEETVDFIPNYDGRVQEPT
VLPSRFPNLLANGSGGIAVGMATNIPPHNLRELADAVFWALENHDADEEE
TLAAVMGRVKGPDFPTAGLIVGSQGTADAYKTGRGSIRMRGVVEVEEDSR
GRTSLVITELPYQVNHDNFITSIAEQVRDGKLAGISNIEDQSSDRVGLRI
VIEIKRDAVAKVVINNLYKHTQLQTSFGANMLAIVDGVPRTLRLDQLIRY
YVDHQLDVIVRRTTYRLRKANERAHILRGLVKALDALDEVIALIRASETV
DIARAGLIELLDIDEIQAQAILDMQLRRLAALERQRIIDDLAKIEAEIAD
LEDILAKPERQRGIVRDELAEIVDRHGDDRRTRIIAI
3D structure
PDB5btc Crystal structure and stability of gyrase-fluoroquinolone cleaved complexes from Mycobacterium tuberculosis.
ChainA
Resolution2.55 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 R39 V51 H52 H85 H87 R98 I181 R25 V37 H38 H71 H73 R84 I167
BS02 dna A Y28 R128 Y129 I181 G184 M185 Y14 R114 Y115 I167 G170 M171
BS03 dna A R39 H52 H85 H87 R98 I181 R25 H38 H71 H73 R84 I167
BS04 dna A Y28 R128 Y129 I181 A182 G184 M185 Y14 R114 Y115 I167 A168 G170 M171
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:5btc, PDBe:5btc, PDBj:5btc
PDBsum5btc
PubMed26792525
UniProtP9WG47|GYRA_MYCTU DNA gyrase subunit A (Gene Name=gyrA)

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