1q4g >> Prostaglandin H2 synthase-1 |
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Hydrophobic Thickness or Depth | 8.9 Å |
Tilt Angle | 90° |
ΔGtransfer | -43.4 kcal/mol |
Links to 1q4g | PDB Sum, PDB, MSD, MMDB |
Topology | lumenal side |
Resolution | 2.0 |
Primary PDB represention | 1q4g |
Other PDB entries representing this structure | 1cqe (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 structures | 0 |
Membranome | |
Uniprot | PGH1_SHEEP |
  | lumenal side |
cytoplasmic side |
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 |
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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 |
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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 |