1t5f
From Proteopedia
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|PDB= 1t5f |SIZE=350|CAPTION= <scene name='initialview01'>1t5f</scene>, resolution 2.20Å | |PDB= 1t5f |SIZE=350|CAPTION= <scene name='initialview01'>1t5f</scene>, resolution 2.20Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=DHH:(S)-2-AMINO-7,7-DIHYDROXYHEPTANOIC+ACID'>DHH</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Arginase Arginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.1 3.5.3.1] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Arginase Arginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.1 3.5.3.1] </span> |
|GENE= ARG1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | |GENE= ARG1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t5f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t5f OCA], [http://www.ebi.ac.uk/pdbsum/1t5f PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1t5f RCSB]</span> | ||
}} | }} | ||
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[[Category: Christianson, D W.]] | [[Category: Christianson, D W.]] | ||
[[Category: Shin, H.]] | [[Category: Shin, H.]] | ||
| - | [[Category: DHH]] | ||
| - | [[Category: MN]] | ||
[[Category: aoh]] | [[Category: aoh]] | ||
[[Category: arginase]] | [[Category: arginase]] | ||
| - | ''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 23:51:36 2008'' |
Revision as of 20:51, 30 March 2008
| |||||||
| , resolution 2.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | ARG1 (Rattus norvegicus) | ||||||
| Activity: | Arginase, with EC number 3.5.3.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
arginase I-AOH complex
Overview
Arginase is a binuclear manganese metalloenzyme that catalyzes the hydrolysis of l-arginine to form l-ornithine and urea. Chiral L-amino acids bearing aldehyde side chains have been synthesized in which the electrophilic aldehyde C=O bond is isosteric with the C=N bond of L-arginine. This substitution is intended to facilitate nucleophilic attack by the metal-bridging hydroxide ion upon binding to the arginase active site. Syntheses of the amino acid aldehydes have been accomplished by reduction, oxidation, and Wittig-type reaction with a commercially available derivative of L-glutamic acid. Amino acid aldehydes exhibit inhibition in the micromolar range, and the X-ray crystal structure of arginase I complexed with one of these inhibitors, (S)-2-amino-7-oxoheptanoic acid, has been determined at 2.2 A resolution. In the enzyme-inhibitor complex, the inhibitor aldehyde moiety is hydrated to form the gem-diol: one hydroxyl group bridges the Mn(2+)(2) cluster and donates a hydrogen bond to D128, and the second hydroxyl group donates a hydrogen bond to E277. The binding mode of the neutral gem-diol may mimic the binding of the neutral tetrahedral intermediate and its flanking transition states in arginase catalysis.
About this Structure
1T5F is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Design of amino acid aldehydes as transition-state analogue inhibitors of arginase., Shin H, Cama E, Christianson DW, J Am Chem Soc. 2004 Aug 25;126(33):10278-84. PMID:15315440
Page seeded by OCA on Sun Mar 30 23:51:36 2008
