1gox

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1gox.jpg|left|200px]]<br /><applet load="1gox" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1gox.jpg|left|200px]]
-
caption="1gox, resolution 2.0&Aring;" />
+
 
-
'''REFINED STRUCTURE OF SPINACH GLYCOLATE OXIDASE AT 2 ANGSTROMS RESOLUTION'''<br />
+
{{Structure
 +
|PDB= 1gox |SIZE=350|CAPTION= <scene name='initialview01'>1gox</scene>, resolution 2.0&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene> and <scene name='pdbligand=FMN:FLAVIN MONONUCLEOTIDE'>FMN</scene>
 +
|ACTIVITY= [http://en.wikipedia.org/wiki/(S)-2-hydroxy-acid_oxidase (S)-2-hydroxy-acid oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.15 1.1.3.15]
 +
|GENE=
 +
}}
 +
 
 +
'''REFINED STRUCTURE OF SPINACH GLYCOLATE OXIDASE AT 2 ANGSTROMS RESOLUTION'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1GOX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea] with <scene name='pdbligand=ACE:'>ACE</scene> and <scene name='pdbligand=FMN:'>FMN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/(S)-2-hydroxy-acid_oxidase (S)-2-hydroxy-acid oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.15 1.1.3.15] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GOX OCA].
+
1GOX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GOX OCA].
==Reference==
==Reference==
-
Refined structure of spinach glycolate oxidase at 2 A resolution., Lindqvist Y, J Mol Biol. 1989 Sep 5;209(1):151-66. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2681790 2681790]
+
Refined structure of spinach glycolate oxidase at 2 A resolution., Lindqvist Y, J Mol Biol. 1989 Sep 5;209(1):151-66. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2681790 2681790]
[[Category: (S)-2-hydroxy-acid oxidase]]
[[Category: (S)-2-hydroxy-acid oxidase]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 19: Line 28:
[[Category: oxidoreductase (oxygen(a))]]
[[Category: oxidoreductase (oxygen(a))]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:52:24 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:26:01 2008''

Revision as of 09:26, 20 March 2008


PDB ID 1gox

Drag the structure with the mouse to rotate
, resolution 2.0Å
Ligands: and
Activity: (S)-2-hydroxy-acid oxidase, with EC number 1.1.3.15
Coordinates: save as pdb, mmCIF, xml



REFINED STRUCTURE OF SPINACH GLYCOLATE OXIDASE AT 2 ANGSTROMS RESOLUTION


Overview

The amino acid sequence of glycolate oxidase from spinach has been fitted to an electron density map of 2.0 A nominal resolution and the structure has been refined using the restrained parameter least-squares refinement of Hendrickson and Konnert. A final crystallographic R-factor of 18.9% was obtained for 32,888 independent reflections from 5.5 to 2 A resolution. The geometry of the model, consisting of 350 amino acid residues, the cofactor flavin mononucleotide and 298 solvent molecules, is close to ideal with root-mean-square deviations of 0.015 A in bond lengths and 2.6 degrees in bond angles. The expected trimodal distribution with preference for staggered conformation is obtained for the side-chain chi 1-angles. The core of the subunit is built up from the eight beta-strands in the beta/alpha-barrel. This core consists of two hydrophobic layers. One in the center is made up of residues pointing in from the beta-strands towards the barrel axis and the second, consisting of two segments of residues, pointing out from the beta-strands towards the eight alpha-helices of the barrel and pointing from the helices towards the strands. The hydrogen bond pattern for the beta-strands in the beta/alpha-barrel is described. There are a number of residues with 3(10)-helix conformation, in particular there is one left-handed helix. The ordered solvent molecules are organized mainly in clusters. The average isotropic temperature factor is quite high, 27.1 A2, perhaps a reflection of the high solvent content in the crystal. The octameric glycolate oxidase molecule, which has 422 symmetry, makes strong interactions around the 4-fold axis forming a tight tetramer, but only weak interactions between the two tetramers forming the octamer.

About this Structure

1GOX is a Single protein structure of sequence from Spinacia oleracea. Full crystallographic information is available from OCA.

Reference

Refined structure of spinach glycolate oxidase at 2 A resolution., Lindqvist Y, J Mol Biol. 1989 Sep 5;209(1):151-66. PMID:2681790

Page seeded by OCA on Thu Mar 20 11:26:01 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools