1lxt

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1lxt.gif|left|200px]]<br /><applet load="1lxt" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1lxt.gif|left|200px]]
-
caption="1lxt, resolution 2.7&Aring;" />
+
 
-
'''STRUCTURE OF PHOSPHOTRANSFERASE PHOSPHOGLUCOMUTASE FROM RABBIT'''<br />
+
{{Structure
 +
|PDB= 1lxt |SIZE=350|CAPTION= <scene name='initialview01'>1lxt</scene>, resolution 2.7&Aring;
 +
|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> and <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]
 +
|GENE=
 +
}}
 +
 
 +
'''STRUCTURE OF PHOSPHOTRANSFERASE PHOSPHOGLUCOMUTASE FROM RABBIT'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1LXT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with <scene name='pdbligand=CD:'>CD</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Known structural/functional Sites: <scene name='pdbsite=MBA:Metal+Binding+Site'>MBA</scene> and <scene name='pdbsite=MBB:Metal+Binding+Site'>MBB</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LXT OCA].
+
1LXT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LXT OCA].
==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15299905 15299905]
+
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:[http://www.ncbi.nlm.nih.gov/pubmed/15299905 15299905]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
[[Category: Phosphoglucomutase]]
[[Category: Phosphoglucomutase]]
Line 23: Line 32:
[[Category: phosphotransferase]]
[[Category: phosphotransferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:49:27 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:36:25 2008''

Revision as of 10:36, 20 March 2008


PDB ID 1lxt

Drag the structure with the mouse to rotate
, resolution 2.7Å
Sites: and
Ligands: and
Activity: Phosphoglucomutase, with EC number 5.4.2.2
Coordinates: save as pdb, mmCIF, xml



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 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 Structure

1LXT is a Single protein structure of sequence from Oryctolagus cuniculus. 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 Thu Mar 20 12:36:25 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools