PDB ID or protein name

7ahl » Alpha-hemolysin

7ahl » Alpha-hemolysin
Magnify 7ahl » Alpha-hemolysinEnlarged view of image
3D view in Jmol or Webmol

gray dot

Download Coordinates

gray dot

Topology in Secreted
Topologyout side
in side
7ahl » Alpha-hemolysin
Hydrophobic Thickness 23.5 ± 0.9 Å
Tilt Angle 0 ± 1°
ΔGtransfer -49.3 kcal/mol
Links to 7ahl PDB Sum, PDB, SCOP, MSD, OCA, MMDB
Topology subunit A (N-terminus out)
Resolution 1.89 Å
Other PDB entries representing this structure 3anz, 3m2l, 3m3r, 3m4d, 3m4e, 4p24, 4yhd
Number of TM Secondary Structures 14
7 transmembrane subunits
A - Tilt: 33° - Segments: 1(119-126), 2(132-140)
B - Tilt: 34° - Segments: 1(119-126), 2(132-140)
C - Tilt: 34° - Segments: 1(119-126), 2(132-140)
D - Tilt: 34° - Segments: 1(119-126), 2(132-140)
E - Tilt: 35° - Segments: 1(119-126), 2(132-140)
F - Tilt: 34° - Segments: 1(119-126), 2(132-140)
G - Tilt: 34° - Segments: 1(119-126), 2(132-140)
Experimental Verification for 7ahl » Alpha-hemolysin
Several Trp residues of alpha-hemolysin (7ahl) are situated in the lipid head group area according to our results, which is consistent with their accessibility to water-soluble iodide and doxyl probes (Raja et al. 1999) and with locations of lipid head groups determined crystallographically (Galdiero and Gouaux 2004).
2 references
Galdiero S, Gouaux E. 2004. Protein Sci. 13:1503-1511. PubMed
Raja SM, Rawat SS, Chattopadhyay A, and Lala AK (1999) Localization and environment of tryptophans in soluble and membrane-bound states of a pore-forming toxin from Staphylococcus aureus. Biophys. J. 76: 1469-1479. PubMed