1dhp

OverviewOverview

The crystal structure of dihydrodipicolinate synthase from E. coli was, determined by multiple isomorphous replacement methods. The structure was, refined at a resolution of 2.5 A and the final R-factor is 19.6% for, 32,190 reflections between 10.0 A and 2.5 A and F > 2 sigma (F). The, crystallographic asymmetric unit contains two monomers related by, approximate 2-fold symmetry. A tetramer with approximate 222 symmetry is, built up by crystallographic symmetry. The tetramer is almost planar with, no contacts between the subunits related by the non-crystallographic dyad., The active sites are accessible from a wide water-filled channel in the, center of the tetramer. The dihydrodipicolinate synthase monomer is, composed of two domains. Each polypeptide chain is folded into an 8-fold, ... [(full description)]

About this StructureAbout this Structure

1DHP is a [Single protein] structure of sequence from [Escherichia coli] with K as [ligand]. Active as [Dihydrodipicolinate synthase], with EC number [4.2.1.52]. Structure known Active Site: S1. Full crystallographic information is available from [OCA].

ReferenceReference

The crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2.5 A resolution., Mirwaldt C, Korndorfer I, Huber R, J Mol Biol. 1995 Feb 10;246(1):227-39. PMID:7853400

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