2vb1
From Proteopedia
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| - | [[Image:2vb1.jpg|left|200px]]<br /><applet load="2vb1" size=" | + | [[Image:2vb1.jpg|left|200px]]<br /><applet load="2vb1" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2vb1, resolution 0.65Å" /> | caption="2vb1, resolution 0.65Å" /> | ||
'''HEWL AT 0.65 ANGSTROM RESOLUTION'''<br /> | '''HEWL AT 0.65 ANGSTROM RESOLUTION'''<br /> | ||
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| + | ==Overview== | ||
| + | The crystal structure of triclinic hen egg-white lysozyme (HEWL) has been, refined against diffraction data extending to 0.65 A resolution measured, at 100 K using synchrotron radiation. Refinement with anisotropic, displacement parameters and with the removal of stereochemical restraints, for the well ordered parts of the structure converged with a conventional, R factor of 8.39% and an R(free) of 9.52%. The use of full-matrix, refinement provided an estimate of the variances in the derived, parameters. In addition to the 129-residue protein, a total of 170 water, molecules, nine nitrate ions, one acetate ion and three ethylene glycol, molecules were located in the electron-density map. Eight sections of the, main chain and many side chains were modeled with alternate conformations., The occupancies of the water sites were refined and this step is, meaningful when assessed by use of the free R factor. A detailed, description and comparison of the structure are made with reference to the, previously reported triclinic HEWL structures refined at 0.925 A (at the, low temperature of 120 K) and at 0.95 A resolution (at room temperature). | ||
==About this Structure== | ==About this Structure== | ||
| - | 2VB1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with ACT, NO3 and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Known structural/functional | + | 2VB1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with <scene name='pdbligand=ACT:'>ACT</scene>, <scene name='pdbligand=NO3:'>NO3</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Known structural/functional Sites: <scene name='pdbsite=AC1:Act Binding Site For Chain A'>AC1</scene>, <scene name='pdbsite=AC2:Edo Binding Site For Chain A'>AC2</scene>, <scene name='pdbsite=AC3:Edo Binding Site For Chain A'>AC3</scene>, <scene name='pdbsite=AC4:Edo Binding Site For Chain A'>AC4</scene>, <scene name='pdbsite=AC5:No3 Binding Site For Chain A'>AC5</scene>, <scene name='pdbsite=AC6:No3 Binding Site For Chain A'>AC6</scene>, <scene name='pdbsite=AC7:No3 Binding Site For Chain A'>AC7</scene>, <scene name='pdbsite=AC8:No3 Binding Site For Chain A'>AC8</scene>, <scene name='pdbsite=AC9:No3 Binding Site For Chain A'>AC9</scene>, <scene name='pdbsite=BC1:No3 Binding Site For Chain A'>BC1</scene>, <scene name='pdbsite=BC2:No3 Binding Site For Chain A'>BC2</scene>, <scene name='pdbsite=BC3:No3 Binding Site For Chain A'>BC3</scene> and <scene name='pdbsite=BC4:No3 Binding Site For Chain A'>BC4</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VB1 OCA]. |
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| + | ==Reference== | ||
| + | Triclinic lysozyme at 0.65 A resolution., Wang J, Dauter M, Alkire R, Joachimiak A, Dauter Z, Acta Crystallogr D Biol Crystallogr. 2007 Dec;63(Pt 12):1254-68. Epub 2007, Nov 16. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18084073 18084073] | ||
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
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[[Category: triclinic hewl]] | [[Category: triclinic hewl]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:24:37 2008'' |
Revision as of 09:24, 23 January 2008
|
HEWL AT 0.65 ANGSTROM RESOLUTION
Overview
The crystal structure of triclinic hen egg-white lysozyme (HEWL) has been, refined against diffraction data extending to 0.65 A resolution measured, at 100 K using synchrotron radiation. Refinement with anisotropic, displacement parameters and with the removal of stereochemical restraints, for the well ordered parts of the structure converged with a conventional, R factor of 8.39% and an R(free) of 9.52%. The use of full-matrix, refinement provided an estimate of the variances in the derived, parameters. In addition to the 129-residue protein, a total of 170 water, molecules, nine nitrate ions, one acetate ion and three ethylene glycol, molecules were located in the electron-density map. Eight sections of the, main chain and many side chains were modeled with alternate conformations., The occupancies of the water sites were refined and this step is, meaningful when assessed by use of the free R factor. A detailed, description and comparison of the structure are made with reference to the, previously reported triclinic HEWL structures refined at 0.925 A (at the, low temperature of 120 K) and at 0.95 A resolution (at room temperature).
About this Structure
2VB1 is a Single protein structure of sequence from Gallus gallus with , and as ligands. Active as Lysozyme, with EC number 3.2.1.17 Known structural/functional Sites: , , , , , , , , , , , and . Full crystallographic information is available from OCA.
Reference
Triclinic lysozyme at 0.65 A resolution., Wang J, Dauter M, Alkire R, Joachimiak A, Dauter Z, Acta Crystallogr D Biol Crystallogr. 2007 Dec;63(Pt 12):1254-68. Epub 2007, Nov 16. PMID:18084073
Page seeded by OCA on Wed Jan 23 11:24:37 2008
Categories: Gallus gallus | Lysozyme | Single protein | Alkire, R. | Dauter, M. | Dauter, Z. | Joachimiak, A. | Wang, J. | ACT | EDO | NO3 | Allergen | Antimicrobial | Atomic resolution | Bacteriolytic enzyme | Glycosidase | Hydrolase | Triclinic hewl
