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6FXQ

Structure of coproheme decarboxylase from Listeria monocytogenes during turnover

Summary for 6FXQ
Entry DOI10.2210/pdb6fxq/pdb
DescriptorPutative heme-dependent peroxidase lmo2113, SODIUM ION, 1,3,5,8-TETRAMETHYL-PORPHINE-2,4,6,7-TETRAPROPIONIC ACID FERROUS COMPLEX, ... (6 entities in total)
Functional Keywordscoproheme decarboxylase, iron coproporphyrin iii, monovinyl monopropionate deuteroheme, oxidoreductase
Biological sourceListeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Total number of polymer chains5
Total formula weight151200.54
Authors
Hofbauer, S.,Pfanzagl, V.,Mlynek, G.,Puehringer, D. (deposition date: 2018-03-09, release date: 2019-07-10, Last modification date: 2024-01-17)
Primary citationMilazzo, L.,Gabler, T.,Puhringer, D.,Jandova, Z.,Maresch, D.,Michlits, H.,Pfanzagl, V.,Djinovic-Carugo, K.,Oostenbrink, C.,Furtmuller, P.G.,Obinger, C.,Smulevich, G.,Hofbauer, S.
Redox Cofactor Rotates during Its Stepwise Decarboxylation: Molecular Mechanism of Conversion of Coproheme to Hemeb.
Acs Catalysis, 9:6766-6782, 2019
Cited by
PubMed: 31423350
DOI: 10.1021/acscatal.9b00963
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.69 Å)
Structure validation

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