Structure of PDB 1j7u Chain A

Receptor sequence
>1j7uA (length=263) Species: 1351 (Enterococcus faecalis) [Search protein sequence]
AKMRISPELKKLIEKYRCVKDTEGMSPAKVYKLVGENENLYLKMTDSRYK
GTTYDVEREKDMMLWLEGKLPVPKVLHFERHDGWSNLLMSEADGVLCSEE
YEDEQSPEKIIELYAECIRLFHSIDISDCPYTNSLDSRLAELDYLLNNDL
ADVDCENWEEDTPFKDPRELYDFLKTEKPEEELVFSHGDLGDSNIFVKDG
KVSGFIDLGRSGRADKWYDIAFCVRSIREDIGEEQYVELFFDLLGIKPDW
EKIKYYILLDELF
3D structure
PDB1j7u Structural analyses of nucleotide binding to an aminoglycoside phosphotransferase.
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) K44 D190 N195 D208
Catalytic site (residue number reindexed from 1) K43 D189 N194 D207
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 MG A N195 D208 N194 D207
BS02 ANP A D22 S27 Y42 K44 A93 F197 I207 D208 D21 S26 Y41 K43 A92 F196 I206 D207
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

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:1j7u, PDBe:1j7u, PDBj:1j7u
PDBsum1j7u
PubMed11467935
UniProtP0A3Y5|KKA3_ENTFL Aminoglycoside 3'-phosphotransferase (Gene Name=aphA)

[Back to BioLiP]