2agv >> Calcium ATPase, E2 state (Ca-free), conformation 1
Hydrophobic Thickness or Depth29.7 Å
Tilt Angle20°
ΔGtransfer-61.5 kcal/mol
Links to 2agvPDB Sum, PDB, MSD, MMDB, Encompass
Topologysubunit A (N terminus cytoplasmic side)
Resolution2.4
Primary PDB represention2agv
Other PDB entries representing this structure1iwo (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 structures10
Membranome
UniprotAT2A1_RABIT
Topology in Endoplasmic reticulum membrane
lumenal side
cytoplasmic side
3D view in GLMol | LiteMol | Jmol | iCn3D

Comments: Similar conformational states are indicated as related PDB entries

Verification: Calcium ATPase, E2 state (Ca-free), conformation 1
Results are consistent with data about biological activity of ATPase in bilayers of various hydrophobic thicknesses (Cornea and Thomas 1994, Lee 1998).
Subunits: 1
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
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