1lxt: Difference between revisions
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|PDB= 1lxt |SIZE=350|CAPTION= <scene name='initialview01'>1lxt</scene>, resolution 2.7Å | |PDB= 1lxt |SIZE=350|CAPTION= <scene name='initialview01'>1lxt</scene>, resolution 2.7Å | ||
|SITE= <scene name='pdbsite=MBA:Metal+Binding+Site'>MBA</scene> and <scene name='pdbsite=MBB:Metal+Binding+Site'>MBB</scene> | |SITE= <scene name='pdbsite=MBA:Metal+Binding+Site'>MBA</scene> and <scene name='pdbsite=MBB:Metal+Binding+Site'>MBB</scene> | ||
|LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene> | |LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Phosphoglucomutase Phosphoglucomutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.2 5.4.2.2] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoglucomutase Phosphoglucomutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.2 5.4.2.2] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lxt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lxt OCA], [http://www.ebi.ac.uk/pdbsum/1lxt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lxt RCSB]</span> | |||
}} | }} | ||
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[[Category: Junior, W J.Ray.]] | [[Category: Junior, W J.Ray.]] | ||
[[Category: Liu, Y.]] | [[Category: Liu, Y.]] | ||
[[Category: dephosphoform]] | [[Category: dephosphoform]] | ||
[[Category: phosphoglucomutase]] | [[Category: phosphoglucomutase]] | ||
[[Category: phosphotransferase]] | [[Category: phosphotransferase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:08:39 2008'' |
Revision as of 22:08, 30 March 2008
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, resolution 2.7Å | |||||||
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Sites: | and | ||||||
Ligands: | , | ||||||
Activity: | Phosphoglucomutase, with EC number 5.4.2.2 | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
STRUCTURE OF PHOSPHOTRANSFERASE PHOSPHOGLUCOMUTASE FROM RABBIT
OverviewOverview
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 sphere of the active-site Mg2+, where the enzymic phosphate group acts as a bidentate ligand; a pair of arginine residues in domain IV that form part of the enzymic phosphate-binding site (distal subsite) whose disposition in the two monomers of the asymmetric unit is affected unequally by distant crystallographic contacts; structural differences throughout domain IV, produced by these differing contacts, that may mimic solution differences induced by substrate binding; large differences in individually refined Debye-Waller thermal factors for corresponding main-chain atoms in monomers (1) and (2), suggesting a dynamic disorder within the crystal that may involve domain-size groups of residues; and a 'nucleophilic elbow' in the active site that resides in a topological environment differing from previous descriptions of this type of structure in other proteins.
About this StructureAbout this Structure
1LXT is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.
ReferenceReference
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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