PDB ID or protein name

1l4v » Sapecin

1l4v » Sapecin
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Topology in Secreted
Topologyout side
in side
1l4v » Sapecin
Depth 5.4 ± 1.5 Å
Tilt Angle 84 ± 18°
ΔGtransfer -5.1 kcal/mol
Links to 1l4v 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 1l4v » Sapecin
The following residues are buried from water in the membrane, according to NMR study: L5, G8, G10-H13, A15-A18, C20-L22, and G27-Y29 (Takeuchi et al. 2004). The following residues are buried in the hydrophobic slab according to the calculations: L6-H19 and L21-L22 (based on locations of NH hydrogens), whereas G27-Y29 segment occupies interfacial region near the calculated hydrophobic boundary.
1 reference
Takeuchi K, Takahashi H, Sugai M, Iwai H, Kohno T, Sekimizu K, Natori S, Shimada I. 2004. Channel-forming membrane permeabilization by an antibacterial protein, sapecin: determination of membrane-buried and oligomerization surfaces by NMR. J Biol Chem. 279: 4981-4987. PubMed
Comments on 1l4v » Sapecin
Sapesin of Sarcophaga peregrina (1l4v) and defensin A of Phormia terranovae (1ica) differ only by a single A34G substitution.