2agv >> Calcium ATPase, E2 state (Ca-free), conformation 1 |
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Hydrophobic Thickness or Depth | 29.7 Å |
Tilt Angle | 20° |
ΔGtransfer | -61.5 kcal/mol |
Links to 2agv | PDB Sum, PDB, MSD, MMDB, Encompass |
Topology | subunit A (N terminus cytoplasmic side) |
Resolution | 2.4 |
Primary PDB represention | 2agv |
Other PDB entries representing this structure | 1iwo (3.1), 2dqs (2.5), 3ar3 (2.3), 3ar4 (2.15), 3ar5 (2.2), 3ar6 (2.2), 3ar7 (2.15), 3w5c (2.5), 3w5d (2.45), 5xab (3.2), 5zmv (3.3) |
Number of TM secondary structures | 10 |
Membranome | |
Uniprot | AT2A1_RABIT |
  | lumenal side |
cytoplasmic side |
Comments: Similar conformational states are indicated as related PDB entries
Verification: Calcium ATPase, E2 state (Ca-free), conformation 1 |
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Results are consistent with data about biological activity of ATPase in bilayers of various hydrophobic thicknesses (Cornea and Thomas 1994, Lee 1998). |
Subunits: 1 |
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A - Tilt: 21 - TM segments: 1(60-77),2(89-103),3(259-274),4(288-306),5(762-780),6(789-807),7(832-853),8(896-915),9(932-949),10(967-986) | |
References: 2 |
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Lee AG (1998) How lipids interact with an intrinsic membrane protein: the case of the calcium pump. Biochim. Biophys. Acta 1376: 381-390. PubMed |
Cornea RL, and Thomas DD (1994) Effect of membrane thickness on the molecular dynamics and enzymatic activity of reconstituted Ca-ATPase. Biochemistry 33: 2912-2920. PubMed |