Orientations of Proteins in Membranes (OPM) database

1sfr » Antigen 85a

See all membrane protein images in OPM

OPM provides spatial arrangements of membrane proteins with respect to the hydrocarbon core of the lipid bilayer.

OPM includes all unique experimental structures of transmembrane proteins and some peripheral proteins and membrane-active peptides (Features).

Each protein is positioned in a hydrophobic slab of adjustable thickness by minimizing its transfer energy from water to the membrane core (Methods).

OPM provides structural classification and sorting according to different criteria (Classification).

Our calculations are in agreement with experimental studies of 24 transmembrane and 39 peripheral peptides and proteins (Comparison with Experiments).

In citing the Orientations of Proteins in Membranes (OPM) database please refer to

Lomize MA, Lomize AL, Pogozheva ID, Mosberg HI (2006) OPM: Orientations of Proteins in Membranes database. Bioinformatics 22, 623-625. PDF PubMed

For an explanation of our method please refer to

Lomize AL, Pogozheva ID, Lomize MA, Mosberg HI (2006) Positioning of proteins in membranes: A computational approach. Protein Science 15, 1318-1333. PDF PubMed

For more information on peripheral proteins please refer to

Lomize AL, Pogozheva ID, Lomize MA, Mosberg HI (2007) The role of hydrophobic interactions in positioning of peripheral proteins in membranes. BMC Struct Biol 7, 44. PDF PubMed

OPM Statistics and Questions

1. Membrane protein not in OPM?

Send us the PDB id with a reference if possible.

2. Calculate orientation for unreleased structure?

We can process your coordinates through email (almz@umich.edu). All information will be kept confidential. Orientation of membrane protein cannot be predicted if all its membrane-anchoring elements are missing or disordered.

3. Errors in orientation or experimental verification description?

Please contact us.

195 (857) Transmembrane (TM) proteins