PDB ID or protein name

1q4g » Prostaglandin H2 synthase-1

1q4g » Prostaglandin H2 synthase-1
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Topology in Endoplasmic reticulum membrane
Topologylumenal side
cytoplasmic side
1q4g » Prostaglandin H2 synthase-1
Depth 8.9 ± 0.4 Å
Tilt Angle 90 ± 1°
ΔGtransfer -43.4 kcal/mol
Links to 1q4g PDB Sum, PDB, SCOP, MSD, OCA, MMDB
Topology lumenal
Resolution 2.0 Å
Other PDB entries representing this structure 1cqe, 1diy, 1ebv, 1eqg, 1eqh, 1fe2, 1ht5, 1ht8, 1igx, 1igz, 1pge, 1pgf, 1pgg, 1prh, 1pth, 1u67, 2ayl, 2oye, 2oyu, 3kk6, 3n8v, 3n8w, 3n8x, 3n8y, 3n8z, 4o1z, 5fdq
Number of subunits 2
Experimental Verification for 1q4g » 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).
2 references
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
Comments on 1q4g » Prostaglandin H2 synthase-1
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).