1lxt
From Proteopedia
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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 [Phosphoglucomutase], with EC number [5.4.2.2]. Structure known Active Sites: MBA and MBB. 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
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