3eca
From Proteopedia
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|PDB= 3eca |SIZE=350|CAPTION= <scene name='initialview01'>3eca</scene>, resolution 2.4Å | |PDB= 3eca |SIZE=350|CAPTION= <scene name='initialview01'>3eca</scene>, resolution 2.4Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ASP:ASPARTIC ACID'>ASP</scene> | + | |LIGAND= <scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Asparaginase Asparaginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.1 3.5.1.1] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Asparaginase Asparaginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.1 3.5.1.1] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3eca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eca OCA], [http://www.ebi.ac.uk/pdbsum/3eca PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3eca RCSB]</span> | ||
}} | }} | ||
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[[Category: Swain, A L.]] | [[Category: Swain, A L.]] | ||
[[Category: Wlodawer, A.]] | [[Category: Wlodawer, A.]] | ||
| - | [[Category: ASP]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''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 05:33:02 2008'' |
Revision as of 02:33, 31 March 2008
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| , resolution 2.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Asparaginase, with EC number 3.5.1.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF ESCHERICHIA COLI L-ASPARAGINASE, AN ENZYME USED IN CANCER THERAPY
Overview
The crystal structure of Escherichia coli asparaginase II (EC 3.5.1.1), a drug (Elspar) used for the treatment of acute lymphoblastic leukemia, has been determined at 2.3 A resolution by using data from a single heavy atom derivative in combination with molecular replacement. The atomic model was refined to an R factor of 0.143. This enzyme, active as a homotetramer with 222 symmetry, belongs to the class of alpha/beta proteins. Each subunit has two domains with unique topological features. On the basis of present structural evidence consistent with previous biochemical studies, we propose locations for the active sites between the N- and C-terminal domains belonging to different subunits and postulate a catalytic role for Thr-89.
About this Structure
3ECA is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of Escherichia coli L-asparaginase, an enzyme used in cancer therapy., Swain AL, Jaskolski M, Housset D, Rao JK, Wlodawer A, Proc Natl Acad Sci U S A. 1993 Feb 15;90(4):1474-8. PMID:8434007
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