Structure of PDB 2bkk Chain C

Receptor sequence
>2bkkC (length=262) Species: 1351 (Enterococcus faecalis) [Search protein sequence]
KMRISPELKKLIEKYRSVKDTEGMSPAKVYKLVGENENLYLKMTDSRYKG
TTYDVEREKDMMLWLEGKLPVPKVLHFERHDGWSNLLMSEADGVLCSEEY
EDEQSPEKIIELYAECIRLFHSIDISDCPYTNSLDSRLAELDYLLNNDLA
DVDSENWEEDTPFKDPRELYDFLKTEKPEEELVFSHGDLGDSNIFVKDGK
VSGFIDLGRSGRADKWYDIAFCVRSIREDIGEEQYVELFFDLLGIKPDWE
KIKYYILLDELF
3D structure
PDB2bkk Allosteric Inhibition of Aminoglycoside Phosphotransferase by a Designed Ankyrin Repeat Protein
ChainC
Resolution2.15 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K44 D190 N195 D208
Catalytic site (residue number reindexed from 1) K42 D188 N193 D206
Enzyme Commision number 2.7.1.95: kanamycin kinase.
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 ADP C D22 S27 Y42 K44 M90 E92 A93 F197 I207 D208 D20 S25 Y40 K42 M88 E90 A91 F195 I205 D206
BS02 MG C N195 D208 N193 D206
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0008910 kanamycin kinase activity
GO:0016301 kinase activity
GO:0016773 phosphotransferase activity, alcohol group as acceptor
Biological Process
GO:0016310 phosphorylation
GO:0046677 response to antibiotic

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Molecular Function
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Biological Process
External links
PDB RCSB:2bkk, PDBe:2bkk, PDBj:2bkk
PDBsum2bkk
PubMed16084385
UniProtP0A3Y5|KKA3_ENTFL Aminoglycoside 3'-phosphotransferase (Gene Name=aphA)

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