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.
1lxt
From Proteopedia
|
STRUCTURE OF PHOSPHOTRANSFERASE PHOSPHOGLUCOMUTASE FROM RABBIT
Overview
Data between 6.0 and 2.4 A resolution, collected at 253 K, wer used to, refine a revised atomic model of muscle phosphoglucomutase: final, crystallographic R factor = 16.3% (Rfree = 19.1%); final r.m.s. deviations, from ideal bond lengths and angles = 0.018 A and 3.2 degrees, respectively. Features of the protein that were recognized only in the, revised model include: the disposition of water molecules within, domain-domain interfaces; two ion pairs buried in domain-domain, interfaces, one of which is a structural arginine around which the, active-site phosphoserine loop is wound; the basic architecture of the, active-site 'crevice', which is a groove in a 1(1/3)-turn helix, open at, both ends, that is produced by the interfacing of the four domains; the, distorted hexacoordinate ligand ... [(full description)]
About this Structure
1LXT is a [Single protein] structure of sequence from [Oryctolagus cuniculus] with CD and SO4 as [ligands]. Active as [[1]], with EC number [5.4.2.2]. Full crystallographic information is available from [OCA].
Reference
Structure of rabbit muscle phosphoglucomutase refined at 2.4 A resolution., Liu Y, Ray WJ Jr, Baranidharan S, Acta Crystallogr D Biol Crystallogr. 1997 Jul 1;53(Pt 4):392-405. PMID:15299905
Page seeded by OCA on Mon Oct 29 17:52:31 2007
