Structure of the human M2 muscarinic acetylcholine receptor bound to an antagonist
The structure was published by Haga, K., Kruse, A.C., Asada, H., et al., Kobilka, B.K., Haga, T., and Kobayashi, T., in 2012 in a paper entitled "Structure of the human M2 muscarinic acetylcholine receptor bound to an antagonist." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 3.0 Å and deposited in 2011.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of Human M2 muscarinic acetylcholine, receptor T4 lysozyme fusion protein. This molecule has the UniProt identifier P08172 (ACM2_HUMAN). The sample contained 467 residues which is 98% of the natural sequence. Out of 467 residues 434 were observed and are deposited in the PDB.
It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.
The molecule is most likely monomeric.
The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):