2VOV
An oxidized tryptophan facilitates copper-binding in Methylococcus capsulatus secreted protein MopE. The structure of wild-type MopE to 1.35AA
Summary for 2VOV
Entry DOI | 10.2210/pdb2vov/pdb |
Related | 2VOW 2VOX |
Descriptor | SURFACE-ASSOCIATED PROTEIN, CALCIUM ION, COPPER (II) ION, ... (4 entities in total) |
Functional Keywords | metal-binding protein, oxidized tryptophan, methanotroph bacterium, kunurenine, copper homeostasis, metal binding protein |
Biological source | METHYLOCOCCUS CAPSULATUS |
Total number of polymer chains | 1 |
Total formula weight | 36289.46 |
Authors | Helland, R.,Fjellbirkeland, A.,Karlsen, O.A.,Ve, T.,Lillehaug, J.R.,Jensen, H.B. (deposition date: 2008-02-22, release date: 2008-03-18, Last modification date: 2023-12-13) |
Primary citation | Helland, R.,Fjellbirkeland, A.,Karlsen, O.A.,Ve, T.,Lillehaug, J.R.,Jensen, H.B. An Oxidized Tryptophan Facilitates Copper Binding in Methylococcus Capsulatus-Secreted Protein Mope. J.Biol.Chem., 283:13897-, 2008 Cited by PubMed: 18348978DOI: 10.1074/JBC.M800340200 PDB entries with the same primary citation |
Experimental method |
Structure validation
Download full validation report![Download](/newweb/media/icons/dl.png)
![Download](/newweb/media/icons/dl.png)