PDB ID or protein name

2a0l » Potassium channel KvAP

2a0l » Potassium channel KvAP
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Topology in Archaebacterial membrane
Topologyextracellular side
cytoplasmic side
2a0l » Potassium channel KvAP
Hydrophobic Thickness 29.5 ± 1.1 Å
Tilt Angle 0 ± 0°
ΔGtransfer -100.0 kcal/mol
Links to 2a0l PDB Sum, PDB, SCOP, MSD, OCA, MMDB
Topology subunit A (N-terminus extracellular)
Resolution 3.9 Å
Other PDB entries representing this structure none
Number of TM Secondary Structures 12
4 transmembrane subunits
A - Tilt: 31° - Segments: 1(150-173), 2(183-195), 3(207-229)
B - Tilt: 31° - Segments: 1(150-173), 2(183-195), 3(207-229)
G - Tilt: 31° - Segments: 1(150-173), 2(183-195), 3(207-229)
H - Tilt: 31° - Segments: 1(150-173), 2(183-195), 3(207-229)
2 references
Cuello LG, Cortes DM, Perozo E. 2004. Molecular architecture of the KvAP voltage-dependent K+ channel in a lipid bilayer. Science. 306:491-5. PubMed
Mackinnon R. 2004. Structural biology. Voltage sensor meets lipid membrane. Science. 306:1304-5. PubMed
Comments on 2a0l » Potassium channel KvAP
Three N-terminal helices are misplaced in the crystal structure (Cuello et al. 2004, MacKinnon 2004). They have been excluded during the calculations. The "paddle" penetrate the bilayer core, but key arginines remain in the lipid head group area.