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5MHB

Product-Complex of E.coli 5-Amino Laevulinic Acid Dehydratase

Replaces:  5IC2
Summary for 5MHB
Entry DOI10.2210/pdb5mhb/pdb
DescriptorDelta-aminolevulinic acid dehydratase, 3-[5-(AMINOMETHYL)-4-(CARBOXYMETHYL)-1H-PYRROL-3-YL]PROPANOIC ACID, ZINC ION, ... (5 entities in total)
Functional Keywordsdehydratase, lyase, tetrapyrrole biosynthesis
Biological sourceEscherichia coli
Total number of polymer chains1
Total formula weight36367.54
Authors
Norton, E.,Erskine, P.T.,Shoolingin-Jordan, P.M.,Cooper, J.B. (deposition date: 2016-11-23, release date: 2016-12-07, Last modification date: 2024-01-17)
Primary citationMills-Davies, N.,Butler, D.,Norton, E.,Thompson, D.,Sarwar, M.,Guo, J.,Gill, R.,Azim, N.,Coker, A.,Wood, S.P.,Erskine, P.T.,Coates, L.,Cooper, J.B.,Rashid, N.,Akhtar, M.,Shoolingin-Jordan, P.M.
Structural studies of substrate and product complexes of 5-aminolaevulinic acid dehydratase from humans, Escherichia coli and the hyperthermophile Pyrobaculum calidifontis.
Acta Crystallogr D Struct Biol, 73:9-21, 2017
Cited by
PubMed: 28045381
DOI: 10.1107/S2059798316019525
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

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