| 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 of this protein | 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. |