1r3j >> Potassium channel KcsA
Hydrophobic Thickness or Depth34.8 Å
Tilt Angle
ΔGtransfer-111.0 kcal/mol
Links to 1r3jPDB Sum, PDB, MSD, MMDB, Encompass
Topologysubunit C (N terminus cytoplasmic side)
Resolution1.9
Primary PDB represention1r3j
Other PDB entries representing this structure1bl8 (3.2), 1f6g (NMR), 1j95 (2.8), 1jq1 (NMR), 1jq2 (NMR), 1jvm (2.8), 1k4c (2.0), 1k4d (2.3), 1r3i (2.4), 1r3k (2.8), 1r3l (2.41), 1zwi (2.5), 2atk (2.5), 2bob (2.76), 2boc (3.01), 2dwd (2.6), 2dwe (2.5), 2h8p (2.25), 2hg5 (2.75), 2hjf (2.9), 2hvj (2.75), 2hvk (1.9), 2ih1 (2.4), 2ih3 (1.72), 2itc (3.2), 2itd (2.7), 2jk5 (2.4), 2nlj (2.52), 2p7t (2.05), 2qto (3.2), 2w0f (2.4), 3gb7 (2.85), 3hpl (3.2), 3ifx (3.56), 3iga (2.75), 3ogc (3.8), 3or6 (2.7), 3or7 (2.3), 3stl (2.4), 3stz (2.5), 4lbe (2.75), 4lcu (2.75), 4msw (2.06), 5e1a (3.4), 5ebl (2.3), 5ebm (2.5), 5ebw (2.3), 5ec1 (2.75), 5ec2 (2.3), 5j9p (2.85), 5vkh (2.25), 6nfu (2.09), 6nfv (2.13), 6pa0 (2.05), 6w0a (3.24), 6w0f (2.4), 6w0g (2.6), 6w0h (2.6), 6w0i (2.33), 6w0j (2.5)
Number of TM secondary structures8
Membranome
UniprotIGHG1_MOUSE, IGKC_MOUSE, KCSA_STRLI
Topology in Bacterial Gram-positive plasma membrane
periplasm
cytoplasmic side
3D view in GLMol | LiteMol | Jmol | iCn3D

Comments: 2k1e and 2kb2 are models of a water-soluble analogue; 1jq1 and 1jq2 are NMR models of a shorter segment. Several structures of the channel, which were deposited to the PDB without proper biomatrix (1zwi, 2atk, 2jk5, 2w0f and 3hpl), are taken from the PDBTM database.

Verification: Potassium channel KcsA
Locations of hydrophobic boundary planes are consistent with spin-labeling (Perozo et al. 1998, Cross et al. 1999, Cross and Hubbell 2002) and hydrophobic matching (Williamson et al. 2002, 2003) studies of KcsA. Average tilt of TM helices (31°) is consistent with ATR FTIR data (33°)(Le Coutre et al. 1998).
Subunits: 4
C - Tilt: 28 - TM segments: 1(25-50),2(86-111)
D - Tilt: 28 - TM segments: 1(25-50),2(86-111)
H - Tilt: 28 - TM segments: 1(25-50),2(86-111)
J - Tilt: 28 - TM segments: 1(25-50),2(86-111)
References: 6
Williamson IM, Alvis SJ, East JM, and Lee AG (2002) Interactions of phospholipids with the potassium channel KcsA. Biophys. J. 83: 2026-2038. PubMed
Perozo E, Cortes DM, and Cuello LG (1998) Three-dimensional architecture and gating mechanism of a K+ channel studied by EPR spectroscopy Nature Struct. Biol. 5 (6): 459-469. PubMed
Le Coutre J, Kaback HR, Patel CKN, Heginbotham L, and Miller C (1998) Fourier transform infrared spectroscopy reveals a rigid alpha-helical assembly for the tetrameric Streptomyces lividans K+ channel. Proc. Natl. Acad. Sci. USA 95: 6114-6117. PubMed
Williamson IM, Alvis SJ, East JM, and Lee AG (2003) The potassium channel KcsA and its interaction with the lipid bilayer. Cell Mol. Life Sci. 60: 1581-1590.2. PubMed
Gross A, and Hubbell WL (2002) Identification of protein side chains near the membrane-aqueous interface: A site-directed spin labeling study of KcsA. Biochemistry 41: 1123-1128. PubMed
Gross A, Columbus L, Hideg K, Altenbach C, and Hubbell WL (1999) Structure of the KcsA potassium channel from Streptomyces lividans: A site-directed spin labeling study of the second transmembrane segment. Biochemistry 38: 10324-10335. PubMed