Structure of PDB 1nd4 Chain B

Receptor sequence
>1nd4B (length=255) Species: 573 (Klebsiella pneumoniae) [Search protein sequence]
GSPAAWVERLFGYDWAQQTIGCSDAAVFRLSAQGRPVLFVKTDLSGALNE
LQDEAARLSWLATTGVPCAAVLDVVTEAGRDWLLLGEVPGQDLLSSHLAP
AEKVSIMADAMRRLHTLDPATCPFDHQAKHRIERARTRMEAGLVDQDDLD
EEHQGLAPAELFARLKARMPDGEDLVVTHGDACLPNIMVENGRFSGFIDC
GRLGVADRYQDIALATRDIAEELGGEWADRFLVLYGIAAPDSQRIAFYRL
LDEFF
3D structure
PDB1nd4 The crystal structure of aminoglycoside-3'-phosphotransferase-IIa, an enzyme responsible for antibiotic resistance
ChainB
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K50 D190 N195 D208
Catalytic site (residue number reindexed from 1) K41 D181 N186 D199
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 B N195 D208 N186 D199
BS02 KAN B D157 L158 D159 D190 R211 R226 D227 E230 D261 E262 F264 D148 L149 D150 D181 R202 R217 D218 E221 D252 E253 F255
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
GO:0046872 metal ion binding
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:1nd4, PDBe:1nd4, PDBj:1nd4
PDBsum1nd4
PubMed12628253
UniProtP00552|KKA2_KLEPN Aminoglycoside 3'-phosphotransferase (Gene Name=neo)

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