PDB ID or protein name

1orq » Potassium channel KvAP, complex with Fab

1orq » Potassium channel KvAP, complex with Fab
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Topology in Archaebacterial membrane
Topologyextracellular side
cytoplasmic side
1orq » Potassium channel KvAP, complex with Fab
Hydrophobic Thickness 29.3 ± 1.6 Å
Tilt Angle 0 ± 0°
ΔGtransfer -78.6 kcal/mol
Links to 1orq PDB Sum, PDB, SCOP, MSD, OCA, MMDB
Topology subunit C (N-terminus cytoplasmic)
Resolution 3.20 Å
Other PDB entries representing this structure none
Number of TM Secondary Structures 12
4 transmembrane subunits
C - Tilt: 31° - Segments: 1(153-172), 2(183-195), 3(207-225)
D - Tilt: 31° - Segments: 1(153-172), 2(183-195), 3(207-225)
G - Tilt: 31° - Segments: 1(153-172), 2(183-195), 3(207-225)
J - Tilt: 31° - Segments: 1(153-172), 2(183-195), 3(207-225)
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 1orq » Potassium channel KvAP, complex with Fab
Three N-terminal helices are misplaced in the crystal structure (Cuello et al. 2004, MacKinnon 2004). They have been excluded during the calculations. Hydrophobic boundaries expand and reach the "paddle" in calculations with detergent solvation parameters.