This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1dhp
From Proteopedia
|
DIHYDRODIPICOLINATE SYNTHASE
Overview
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 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].
Reference
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
Page seeded by OCA on Tue Oct 30 15:01:17 2007
