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: 18348978 DOI: 10.1074/JBC.M800340200 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.35 Å)

Structure validation