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1orq » Potassium channel KvAP

• Type: 1. Transmembrane (3 classes)
• Class: 1.1. Alpha-helical polytopic (72 superfamilies)
• Superfamily: 1.1.12. Voltage-gated channel like (3 families) 1.A.1 (TCDB)
• Family: 1.1.12.01. Voltage-gated ion channels (36 proteins) 1.A.1 (TCDB)
• Species: Aeropyrum pernix (4 proteins)
• Localization: Archaebacterial membrane (54 proteins)

1orq » Potassium channel KvAP
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 of this protein	1ors, 2a0l
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
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.

Copyright © 2005-2013 Andrei Lomize, Mikhail Lomize and Irina Pogozheva
University of Michigan, Ann Arbor, MI 48109 USA