1jsw
From Proteopedia
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|PDB= 1jsw |SIZE=350|CAPTION= <scene name='initialview01'>1jsw</scene>, resolution 2.7Å | |PDB= 1jsw |SIZE=350|CAPTION= <scene name='initialview01'>1jsw</scene>, resolution 2.7Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Aspartate_ammonia-lyase Aspartate ammonia-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.1.1 4.3.1.1] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_ammonia-lyase Aspartate ammonia-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.1.1 4.3.1.1] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jsw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jsw OCA], [http://www.ebi.ac.uk/pdbsum/1jsw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jsw RCSB]</span> | ||
}} | }} | ||
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[[Category: Farber, G K.]] | [[Category: Farber, G K.]] | ||
[[Category: Shi, W.]] | [[Category: Shi, W.]] | ||
| - | [[Category: ACT]] | ||
| - | [[Category: GLC]] | ||
[[Category: amino acid ammonia-lyase]] | [[Category: amino acid ammonia-lyase]] | ||
| - | ''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 21:38:30 2008'' |
Revision as of 18:38, 30 March 2008
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| , resolution 2.7Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Aspartate ammonia-lyase, with EC number 4.3.1.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NATIVE L-ASPARTATE AMMONIA LYASE
Overview
The X-ray crystal structure of l-aspartate ammonia-lyase has been determined to 2.8 A resolution. The enzyme contains three domains, and each domain is composed almost completely of alpha helices. The central domain is composed of five long helices. In the tetramer, these five helices form a 20-helix cluster. Such clusters have also been seen in delta-crystallin and in fumarase. The active site of aspartase has been located in a region that contains side chains from three different subunits. The structure of the apoenzyme has made it possible to identify some of the residues that are involved in binding the substrate. These residues have been examined by site-directed mutagenesis, and their putative roles have been assigned [Jayasekera, M. M. K., Shi, W., Farber, G. K., & Viola, R. E. (1997) Biochemistry 36, 9145-9150].
About this Structure
1JSW is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
The structure of L-aspartate ammonia-lyase from Escherichia coli., Shi W, Dunbar J, Jayasekera MM, Viola RE, Farber GK, Biochemistry. 1997 Jul 29;36(30):9136-44. PMID:9230045
Page seeded by OCA on Sun Mar 30 21:38:30 2008
