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5C4L

Conformational alternate of sisomicin in complex with APH(2")-IVa

Summary for 5C4L
Entry DOI10.2210/pdb5c4l/pdb
DescriptorAPH(2'')-Id, (2S,3R)-3-amino-6-(aminomethyl)-3,4-dihydro-2H-pyran-2-ol, (1S,2S,3R,4S,6R)-4,6-diamino-3-{[(2S,3R)-3-amino-6-(aminomethyl)-3,4-dihydro-2H-pyran-2-yl]oxy}-2-hydroxycyclohexyl 3-deoxy-4-C-methyl-3-(methylamino)-beta-L-arabinopyranoside, ... (4 entities in total)
Functional Keywordsaminoglycoside phosphotransferase, antibiotic resistance, transferase
Biological sourceEnterococcus casseliflavus
Total number of polymer chains2
Total formula weight75783.40
Authors
Kaplan, E.,Guichou, J.F.,Berrou, K.,Chaloin, L.,Leban, N.,Lallemand, P.,Barman, T.,Serpersu, E.H.,Lionne, C. (deposition date: 2015-06-18, release date: 2016-02-03, Last modification date: 2024-01-10)
Primary citationKaplan, E.,Guichou, J.F.,Chaloin, L.,Kunzelmann, S.,Leban, N.,Serpersu, E.H.,Lionne, C.
Aminoglycoside binding and catalysis specificity of aminoglycoside 2-phosphotransferase IVa: A thermodynamic, structural and kinetic study.
Biochim.Biophys.Acta, 1860:802-813, 2016
Cited by
PubMed Abstract: Aminoglycoside O-phosphotransferases make up a large class of bacterial enzymes that is widely distributed among pathogens and confer a high resistance to several clinically used aminoglycoside antibiotics. Aminoglycoside 2″-phosphotransferase IVa, APH(2″)-IVa, is an important member of this class, but there is little information on the thermodynamics of aminoglycoside binding and on the nature of its rate-limiting step.
PubMed: 26802312
DOI: 10.1016/j.bbagen.2016.01.016
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.35 Å)
Structure validation

237735

数据于2025-06-18公开中

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