2apj
From Proteopedia
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|GENE= AT4G34215 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana]) | |GENE= AT4G34215 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana]) | ||
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam03629 DUF303]</span> | |DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam03629 DUF303]</span> | ||
- | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2apj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2apj OCA], [http://www.ebi.ac.uk/pdbsum/2apj PDBsum | + | |RELATEDENTRY=[[2aea|2AEA]] |
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2apj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2apj OCA], [http://www.ebi.ac.uk/pdbsum/2apj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2apj RCSB]</span> | ||
}} | }} | ||
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[[Category: structural genomic]] | [[Category: structural genomic]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:55:39 2008'' |
Revision as of 22:55, 30 March 2008
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, resolution 1.600Å | |||||||
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Ligands: | |||||||
Gene: | AT4G34215 (Arabidopsis thaliana) | ||||||
Domains: | DUF303 | ||||||
Related: | 2AEA
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
X-Ray Structure of Protein from Arabidopsis Thaliana AT4G34215 at 1.6 Angstrom Resolution
Overview
The crystal structure of the At4g34215 protein of Arabidopsis thaliana was determined by molecular replacement and refined to an R factor of 14.6% (R(free) = 18.3%) at 1.6 Angstroms resolution. The crystal structure confirms that At4g34215 belongs to the SGNH-hydrolase superfamily of enzymes. The catalytic triad of the enzyme comprises residues Ser31, His238 and Asp235. In this structure the catalytic serine residue was found to be covalently modified, possibly by phenylmethylsulfonyl fluoride. The structure also reveals a previously undescribed variation within the active site. The conserved asparagine from block III, which provides a hydrogen bond for an oxyanion hole in the SGNH-hydrolase superfamily enzymes, is missing in At4g34215 and is functionally replaced by Gln30 from block I. This residue is positioned in a catalytically competent conformation by nearby residues, including Gln159, Gly160 and Glu161, which are fully conserved in the carbohydrate esterase family 6 enzymes.
About this Structure
2APJ is a Single protein structure of sequence from Arabidopsis thaliana. This structure supersedes the now removed PDB entry 2AEA. Full crystallographic information is available from OCA.
Reference
The structure at 1.6 Angstroms resolution of the protein product of the At4g34215 gene from Arabidopsis thaliana., Bitto E, Bingman CA, McCoy JG, Allard ST, Wesenberg GE, Phillips GN Jr, Acta Crystallogr D Biol Crystallogr. 2005 Dec;61(Pt 12):1655-61. Epub 2005, Nov 19. PMID:16301800
Page seeded by OCA on Mon Mar 31 01:55:39 2008
Categories: Arabidopsis thaliana | Single protein | Allard, S T. | Bingman, C A. | Bitto, E. | CESG, Center for Eukaryotic Structural Genomics. | Jr., G N.Phillips. | Mccoy, J G. | Wesenberg, G E. | At4g34215 | Carbohydrate esterase family 6 | Center for eukaryotic structural genomic | Cesg | Protein structure initiative | Psi | Putative esterase,sgnh-hydrolase superfamily | Structural genomic