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5LOQ

Structure of coproheme bound HemQ from Listeria monocytogenes

Summary for 5LOQ
Entry DOI10.2210/pdb5loq/pdb
DescriptorPutative heme-dependent peroxidase lmo2113, SODIUM ION, 1,3,5,8-TETRAMETHYL-PORPHINE-2,4,6,7-TETRAPROPIONIC ACID FERROUS COMPLEX, ... (5 entities in total)
Functional Keywordshemq, heme biosynthesis, coproheme, heme b, gram-positive pathogens, oxidoreductase
Biological sourceListeria monocytogenes
Total number of polymer chains5
Total formula weight147887.97
Authors
Puehringer, D.,Mlynek, G.,Hofbauer, S.,Djinovic-Carugo, K.,Obinger, C. (deposition date: 2016-08-09, release date: 2016-10-26, Last modification date: 2024-01-10)
Primary citationHofbauer, S.,Mlynek, G.,Milazzo, L.,Puhringer, D.,Maresch, D.,Schaffner, I.,Furtmuller, P.G.,Smulevich, G.,Djinovic-Carugo, K.,Obinger, C.
Hydrogen peroxide-mediated conversion of coproheme to heme b by HemQ-lessons from the first crystal structure and kinetic studies.
FEBS J., 283:4386-4401, 2016
Cited by
PubMed: 27758026
DOI: 10.1111/febs.13930
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.69 Å)
Structure validation

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