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1aq6

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|PDB= 1aq6 |SIZE=350|CAPTION= <scene name='initialview01'>1aq6</scene>, resolution 1.95&Aring;
|PDB= 1aq6 |SIZE=350|CAPTION= <scene name='initialview01'>1aq6</scene>, resolution 1.95&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=FMT:FORMIC ACID'>FMT</scene>
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|LIGAND= <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/(S)-2-haloacid_dehalogenase (S)-2-haloacid dehalogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.8.1.2 3.8.1.2]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/(S)-2-haloacid_dehalogenase (S)-2-haloacid dehalogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.8.1.2 3.8.1.2] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1aq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aq6 OCA], [http://www.ebi.ac.uk/pdbsum/1aq6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1aq6 RCSB]</span>
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[[Category: Ridder, I S.]]
[[Category: Ridder, I S.]]
[[Category: Rozeboom, H J.]]
[[Category: Rozeboom, H J.]]
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[[Category: FMT]]
 
[[Category: l-2-haloacid dehalogenase]]
[[Category: l-2-haloacid dehalogenase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:00:56 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:45:24 2008''

Revision as of 15:45, 30 March 2008


PDB ID 1aq6

Drag the structure with the mouse to rotate
, resolution 1.95Å
Ligands:
Activity: (S)-2-haloacid dehalogenase, with EC number 3.8.1.2
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



STRUCTURE OF L-2-HALOACID DEHALOGENASE FROM XANTHOBACTER AUTOTROPHICUS


Overview

The L-2-haloacid dehalogenase from the 1,2-dichloroethane degrading bacterium Xanthobacter autotrophicus GJ10 catalyzes the hydrolytic dehalogenation of small L-2-haloalkanoic acids to yield the corresponding D-2-hydroxyalkanoic acids. Its crystal structure was solved by the method of multiple isomorphous replacement with incorporation of anomalous scattering information and solvent flattening, and was refined at 1.95-A resolution to an R factor of 21.3%. The three-dimensional structure is similar to that of the homologous L-2-haloacid dehalogenase from Pseudomonas sp. YL (1), but the X. autotrophicus enzyme has an extra dimerization domain, an active site cavity that is completely shielded from the solvent, and a different orientation of several catalytically important amino acid residues. Moreover, under the conditions used, a formate ion is bound in the active site. The position of this substrate-analogue provides valuable information on the reaction mechanism and explains the limited substrate specificity of the Xanthobacter L-2-haloacid dehalogenase.

About this Structure

1AQ6 is a Single protein structure of sequence from Xanthobacter autotrophicus. Full crystallographic information is available from OCA.

Reference

Three-dimensional structure of L-2-haloacid dehalogenase from Xanthobacter autotrophicus GJ10 complexed with the substrate-analogue formate., Ridder IS, Rozeboom HJ, Kalk KH, Janssen DB, Dijkstra BW, J Biol Chem. 1997 Dec 26;272(52):33015-22. PMID:9407083

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