5OTM

Crystal structure of human MTH1 in complex with O6-methyl-dGMP

Summary for 5OTM

Entry DOI	10.2210/pdb5otm/pdb
Descriptor	7,8-dihydro-8-oxoguanine triphosphatase, SULFATE ION, ACETATE ION, ... (5 entities in total)
Functional Keywords	mth1, inhibitor, complex, hydrolase, nudix, methylated nucleotide, o6-methyl-dgmp
Biological source	Homo sapiens (Human)
Total number of polymer chains	2
Total formula weight	38057.52
Authors	Gustafsson, R.,Henriksson, L.,Jemth, A.-S.,Brautigam, L.,Carreras Puigvert, J.,Homan, E.,Warpman Berglund, U.,Helleday, T.,Stenmark, P. (deposition date: 2017-08-22, release date: 2018-09-05, Last modification date: 2024-01-17)
Primary citation	Jemth, A.S.,Gustafsson, R.,Brautigam, L.,Henriksson, L.,Vallin, K.S.A.,Sarno, A.,Almlof, I.,Homan, E.,Rasti, A.,Warpman Berglund, U.,Stenmark, P.,Helleday, T. MutT homologue 1 (MTH1) catalyzes the hydrolysis of mutagenic O6-methyl-dGTP. Nucleic Acids Res., 46:10888-10904, 2018 Cited by PubMed: 30304478 DOI: 10.1093/nar/gky896 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.8 Å)

Structure validation