PDB ID or protein name

1t5n » Daptomycin, Ca-bound

1t5n » Daptomycin, Ca-bound
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Topology in Secreted
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1t5n » Daptomycin, Ca-bound
Hydrophobic Thickness or Depth 8.6 ± 2.0 Å
Tilt Angle 21 ± 24°
ΔGtransfer -9.0 kcal/mol
Links to 1t5n PDB Sum, PDB, SCOP, MSD, OCA, MMDB
Topology out
Resolution NMR
Other PDB entries representing this structure none
Number of subunits 1
Experimental Verification for 1t5n » Daptomycin, Ca-bound
Residue Kyn14 is situated at the lipid-water interface and penetrates deeper into the membrane in the Ca-bound state (Lakey and Ptak 1988).
2 references
Jung D, Rozek A, Okon M, Hancock RE. 2004. Structural transitions as determinants of the action of the calcium-dependent antibiotic daptomycin. Chem Biol. 11:949-57. PubMed
Lakey JH, Ptak M. 1988. Fluorescence indicates a calcium-dependent interaction between the lipopeptide antibiotic LY146032 and phospholipid membranes. Biochemistry. 27:4639-45. PubMed
Comments on 1t5n » Daptomycin, Ca-bound
Daptomycin is a cyclic anionic lipopeptide antibiotic recently approved for the treatment of complicated skin infections (Cubicin). Its function is dependent on calcium (as Ca2+). The NMR structure of daptomycin indicated that Ca2+ induced a conformational change in daptomycin that increased its amphipathicity (Jung et al. 2004).