4MLQ
Crystal structure of Bacillus megaterium porphobilinogen deaminase
Summary for 4MLQ
Entry DOI | 10.2210/pdb4mlq/pdb |
Related | 1PDA 4HTG |
Descriptor | Porphobilinogen deaminase, 3-[5-{[3-(2-carboxyethyl)-4-(carboxymethyl)-5-methyl-1H-pyrrol-2-yl]methyl}-4-(carboxymethyl)-1H-pyrrol-3-yl]propanoic acid, 3-[(5S)-5-{[3-(2-carboxyethyl)-4-(carboxymethyl)-5-methyl-1H-pyrrol-2-yl]methyl}-4-(carboxymethyl)-2-oxo-2,5-dihydro-1H-pyrrol-3-yl]propanoic acid, ... (5 entities in total) |
Functional Keywords | tetrapyrrole biosynthesis, porphobilinogen deaminase, dipyrromethane cofactor, three-domain fold, domains 1 and 2 resemble the fold of type ii periplasmic binding proteins, pyrrole polymerisation, transferase |
Biological source | Bacillus megaterium |
Total number of polymer chains | 1 |
Total formula weight | 35429.65 |
Authors | Azim, N.,Deery, E.,Warren, M.J.,Erskine, P.,Cooper, J.B.,Coker, A.,Wood, S.P.,Akhtar, M. (deposition date: 2013-09-06, release date: 2014-04-02) |
Primary citation | Azim, N.,Deery, E.,Warren, M.J.,Wolfenden, B.A.,Erskine, P.,Cooper, J.B.,Coker, A.,Wood, S.P.,Akhtar, M. Structural evidence for the partially oxidized dipyrromethene and dipyrromethanone forms of the cofactor of porphobilinogen deaminase: structures of the Bacillus megaterium enzyme at near-atomic resolution. Acta Crystallogr.,Sect.D, 70:744-751, 2014 Cited by PubMed: 24598743DOI: 10.1107/S139900471303294X PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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