1q4g >> Prostaglandin H2 synthase-1
Hydrophobic Thickness or Depth8.9 Å
Tilt Angle90°
ΔGtransfer-43.4 kcal/mol
Links to 1q4gPDB Sum, PDB, MSD, MMDB
Topologylumenal side
Resolution2.0
Primary PDB represention1q4g
Other PDB entries representing this structure1cqe (3.1), 1diy (3.0), 1ebv (3.2), 1eqg (2.61), 1eqh (2.7), 1fe2 (3.0), 1ht5 (2.75), 1ht8 (2.69), 1igx (3.1), 1igz (2.9), 1pge (3.5), 1pgf (4.5), 1pgg (4.5), 1prh (3.5), 1pth (3.4), 1u67 (3.1), 2ayl (2.0), 2oye (2.85), 2oyu (2.7), 3kk6 (2.75), 3n8v (3.05), 3n8w (2.75), 3n8x (2.75), 3n8y (2.6), 3n8z (2.9), 4o1z (2.4), 5fdq (1.9), 5u6x (2.93), 5wbe (2.75), 7jxt (3.35)
Number of TM secondary structures0
Membranome
UniprotPGH1_SHEEP
Topology in Endoplasmic reticulum membrane
lumenal side
cytoplasmic side
3D view in GLMol | LiteMol | Jmol | iCn3D

Comments: May play an important role in regulating or promoting cell proliferation in some normal and neoplastically transformed cells. Structure with longer polypeptide chain: 1u67 (1-600, 3.1A resolution).

Verification: Prostaglandin H2 synthase-1
Residues I74, W75, W77, L78, F88, F91, L92, W98, L99 and F102 are involved in hydrophobic interactions with the membrane (Spencer et al. 1999) in agreement with the set of membrane core embedded residues in the calculated position of the dimer (I74, W75, W77, L78, T81, L82, F88, F91, L92, W98, L99, F102, V103, T106, F107, I108). Protein was crystallized with N-OCTYL-beta-D-GLUCOPYRANOSIDE. Calculated boundaries correspond to oxygens of several crystallized detergent molecules. Two other molecules of detergent occupy binding pocket. Results of our calculations are also consitent with MD simulations of the protein (Nina et al. 2000).
References: 2
Nina M, Berneche S, Roux B. 2000. Anchoring of a monotopic membrane protein: the binding of prostaglandin H2 synthase-1 to the surface of a phospholipid bilayer. Eur Biophys J. 29:439-54. PubMed
Spencer AG, Thuresson E, Otto JC, Song I, Smith T, DeWitt DL, Garavito RM, Smith WL. 1999 The membrane binding domains of prostaglandin endoperoxide H synthases 1 and 2. Peptide mapping and mutational analysis. J Biol Chem. 274: 32936-32942. PubMed