OPM

UNIVERSITY OF MICHIGAN | COLLEGE OF PHARMACY | LOMIZE GROUP

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Type: Monotopic/peripheral (4 classes)
Class: All alpha monotopic/peripheral (66 superfamilies)
Superfamily: Heme-dependent peroxidases (1 families) PF03098
Family: Haem peroxidase (6 proteins) PF03098 IPR019791 PDBsum
Species: Ovis aries (60 proteins)
Localization: Endoplasmic reticulum membrane (548 proteins)

1q4g >> Prostaglandin H2 synthase-1
Hydrophobic Thickness or Depth	8.9 Å
Tilt Angle	90°
ΔG_transfer	-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

Download OPM File: 1q4g.pdb

PDB Sum, PDB

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).

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