3EMN
The Crystal Structure of Mouse VDAC1 at 2.3 A resolution
Summary for 3EMN
Entry DOI | 10.2210/pdb3emn/pdb |
Descriptor | Voltage-dependent anion-selective channel protein 1, 1,2-DIMYRISTOYL-RAC-GLYCERO-3-PHOSPHOCHOLINE (3 entities in total) |
Functional Keywords | vdac1, eukaryotic membrane protein, beta barrel, channel, apoptosis, ion transport, mitochondrion, outer membrane, phosphoprotein, porin, transmembrane, transport, membrane protein |
Biological source | Mus musculus (Mouse) |
Cellular location | Isoform Mt-VDAC1: Mitochondrion outer membrane; Multi-pass membrane protein. Isoform Pl-VDAC1: Cell membrane; Multi-pass membrane protein: Q60932 |
Total number of polymer chains | 1 |
Total formula weight | 32873.88 |
Authors | Ujwal, R.,Cascio, D.,Colletier, J.-P.,Faham, S.,Zhang, J.,Toro, L.,Ping, P.,Abramson, J. (deposition date: 2008-09-24, release date: 2008-12-16, Last modification date: 2024-02-21) |
Primary citation | Ujwal, R.,Cascio, D.,Colletier, J.P.,Faham, S.,Zhang, J.,Toro, L.,Ping, P.,Abramson, J. The crystal structure of mouse VDAC1 at 2.3 A resolution reveals mechanistic insights into metabolite gating Proc.Natl.Acad.Sci.USA, 105:17742-17747, 2008 Cited by PubMed: 18988731DOI: 10.1073/pnas.0809634105 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
Download full validation report