![]() | extracellular side |
| cytoplasmic side |
| 2bg9 » Nicotinic acetylcholine receptor, closed state | |
|---|---|
| Hydrophobic Thickness | 30.1 ± 1.1 Å |
| Tilt Angle | 3 ± 0° |
| ΔGtransfer | -119.6 kcal/mol |
| Links to 2bg9 | PDB Sum, PDB, SCOP, MSD, OCA, MMDB |
| Topology | subunit A (N-terminus extracellular) |
| Resolution | 4.00 Å |
| Other PDB entries of this protein | 1oed |
| Number of TM Secondary Structures | 20 |
| 5 transmembrane subunits |
|---|
| A - Tilt: 15° - Segments: 1(213-233), 2(244-265), 3(276-297), 4(409-433) |
| B - Tilt: 14° - Segments: 1(220-240), 2(251-271), 3(282-303), 4(438-463) |
| C - Tilt: 10° - Segments: 1(229-249), 2(258-279), 3(289-313), 4(457-479) |
| D - Tilt: 8° - Segments: 1(215-235), 2(244-264), 3(278-299), 4(409-430) |
| E - Tilt: 14° - Segments: 1(221-242), 2(252-273), 3(285-306), 4(449-470) |
| Experimental Verification for 2bg9 » Nicotinic acetylcholine receptor, closed state |
|---|
| The shallow location of Trp452 from the G subunit of the nicotinic acetylcholine receptor (1.4 A° below the calculated hydrophobic boundary) is consistent with fluorescence studies (Chattopadhyay and McNamee 1991). |
| 1 reference |
|---|
| Chattopadhyay A, and McNamee MG (1991) Average membrane penetration depth of tryptophan residues of the nicotinic acetylcholine receptor by the parallax method. Biochemistry 30: 7159-7164. PubMed |