1aq6
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1aq6 |SIZE=350|CAPTION= <scene name='initialview01'>1aq6</scene>, resolution 1.95Å | |PDB= 1aq6 |SIZE=350|CAPTION= <scene name='initialview01'>1aq6</scene>, resolution 1.95Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=FMT:FORMIC ACID'>FMT</scene> | + | |LIGAND= <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene> |
| - | |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] | + | |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= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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> | ||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Ridder, I S.]] | [[Category: Ridder, I S.]] | ||
[[Category: Rozeboom, H J.]] | [[Category: Rozeboom, H J.]] | ||
| - | [[Category: FMT]] | ||
[[Category: l-2-haloacid dehalogenase]] | [[Category: l-2-haloacid dehalogenase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''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
| |||||||
| , 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
Page seeded by OCA on Sun Mar 30 18:45:24 2008
