2v9e

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|PDB= 2v9e |SIZE=350|CAPTION= <scene name='initialview01'>2v9e</scene>, resolution 1.58&Aring;
|PDB= 2v9e |SIZE=350|CAPTION= <scene name='initialview01'>2v9e</scene>, resolution 1.58&Aring;
|SITE= <scene name='pdbsite=AC1:Zn+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Zn+Binding+Site+For+Chain+A'>AC2</scene>, <scene name='pdbsite=AC3:Zn+Binding+Site+For+Chain+A'>AC3</scene>, <scene name='pdbsite=AC4:Zn+Binding+Site+For+Chain+B'>AC4</scene>, <scene name='pdbsite=AC5:Zn+Binding+Site+For+Chain+B'>AC5</scene>, <scene name='pdbsite=AC6:Zn+Binding+Site+For+Chain+B'>AC6</scene>, <scene name='pdbsite=AC7:Act+Binding+Site+For+Chain+A'>AC7</scene>, <scene name='pdbsite=AC8:Act+Binding+Site+For+Chain+A'>AC8</scene>, <scene name='pdbsite=AC9:Act+Binding+Site+For+Chain+A'>AC9</scene>, <scene name='pdbsite=BC1:Act+Binding+Site+For+Chain+A'>BC1</scene> and <scene name='pdbsite=BC2:Act+Binding+Site+For+Chain+B'>BC2</scene>
|SITE= <scene name='pdbsite=AC1:Zn+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Zn+Binding+Site+For+Chain+A'>AC2</scene>, <scene name='pdbsite=AC3:Zn+Binding+Site+For+Chain+A'>AC3</scene>, <scene name='pdbsite=AC4:Zn+Binding+Site+For+Chain+B'>AC4</scene>, <scene name='pdbsite=AC5:Zn+Binding+Site+For+Chain+B'>AC5</scene>, <scene name='pdbsite=AC6:Zn+Binding+Site+For+Chain+B'>AC6</scene>, <scene name='pdbsite=AC7:Act+Binding+Site+For+Chain+A'>AC7</scene>, <scene name='pdbsite=AC8:Act+Binding+Site+For+Chain+A'>AC8</scene>, <scene name='pdbsite=AC9:Act+Binding+Site+For+Chain+A'>AC9</scene>, <scene name='pdbsite=BC1:Act+Binding+Site+For+Chain+A'>BC1</scene> and <scene name='pdbsite=BC2:Act+Binding+Site+For+Chain+B'>BC2</scene>
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=ACT:ACETATE ION'>ACT</scene>
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|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Rhamnulose-1-phosphate_aldolase Rhamnulose-1-phosphate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.19 4.1.2.19]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Rhamnulose-1-phosphate_aldolase Rhamnulose-1-phosphate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.19 4.1.2.19] </span>
|GENE=
|GENE=
 +
|DOMAIN=
 +
|RELATEDENTRY=[[1gt7|1GT7]], [[1ojr|1OJR]], [[2uyu|2UYU]], [[2v2b|2V2B]], [[2uyv|2UYV]], [[2v29|2V29]], [[2v2a|2V2A]], [[2v9f|2V9F]], [[2v9g|2V9G]], [[2v9i|2V9I]], [[2v9l|2V9L]], [[2v9m|2V9M]]
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2v9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v9e OCA], [http://www.ebi.ac.uk/pdbsum/2v9e PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2v9e RCSB]</span>
}}
}}
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[[Category: Grueninger, D.]]
[[Category: Grueninger, D.]]
[[Category: Schulz, G E.]]
[[Category: Schulz, G E.]]
-
[[Category: ACT]]
 
-
[[Category: ZN]]
 
[[Category: 2-ketose degradation]]
[[Category: 2-ketose degradation]]
[[Category: aggregation]]
[[Category: aggregation]]
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[[Category: zinc enzyme]]
[[Category: zinc enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:44:30 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:09:59 2008''

Revision as of 02:10, 31 March 2008


PDB ID 2v9e

Drag the structure with the mouse to rotate
, resolution 1.58Å
Sites: , , , , , , , , , and
Ligands: ,
Activity: Rhamnulose-1-phosphate aldolase, with EC number 4.1.2.19
Related: 1GT7, 1OJR, 2UYU, 2V2B, 2UYV, 2V29, 2V2A, 2V9F, 2V9G, 2V9I, 2V9L, 2V9M


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT E192A-K248W-A273S)


Overview

The analysis of natural contact interfaces between protein subunits and between proteins has disclosed some general rules governing their association. We have applied these rules to produce a number of novel assemblies, demonstrating that a given protein can be engineered to form contacts at various points of its surface. Symmetry plays an important role because it defines the multiplicity of a designed contact and therefore the number of required mutations. Some of the proteins needed only a single side-chain alteration in order to associate to a higher-order complex. The mobility of the buried side chains has to be taken into account. Four assemblies have been structurally elucidated. Comparisons between the designed contacts and the results will provide useful guidelines for the development of future architectures.

About this Structure

2V9E is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Designed protein-protein association., Grueninger D, Treiber N, Ziegler MO, Koetter JW, Schulze MS, Schulz GE, Science. 2008 Jan 11;319(5860):206-9. PMID:18187656

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