1rpa
From Proteopedia
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|PDB= 1rpa |SIZE=350|CAPTION= <scene name='initialview01'>1rpa</scene>, resolution 3.0Å | |PDB= 1rpa |SIZE=350|CAPTION= <scene name='initialview01'>1rpa</scene>, resolution 3.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | + | |LIGAND= <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=TAR:D(-)-TARTARIC+ACID'>TAR</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Acid_phosphatase Acid phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.2 3.1.3.2] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Acid_phosphatase Acid phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.2 3.1.3.2] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rpa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rpa OCA], [http://www.ebi.ac.uk/pdbsum/1rpa PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1rpa RCSB]</span> | ||
}} | }} | ||
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[[Category: Lindqvist, Y.]] | [[Category: Lindqvist, Y.]] | ||
[[Category: Schneider, G.]] | [[Category: Schneider, G.]] | ||
| - | [[Category: NAG]] | ||
| - | [[Category: TAR]] | ||
[[Category: hydrolase(phosphoric monoester)]] | [[Category: hydrolase(phosphoric monoester)]] | ||
| - | ''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 23:31:06 2008'' |
Revision as of 20:31, 30 March 2008
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| , resolution 3.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Activity: | Acid phosphatase, with EC number 3.1.3.2 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THREE-DIMENSIONAL STRUCTURE OF RAT ACID PHOSPHATASE IN COMPLEX WITH L(+) TARTRATE
Overview
The crystal structure of recombinant rat prostatic acid phosphatase in complex with the inhibitor L(+)-tartrate was determined to 3-A resolution with protein crystallographic methods. The inhibitor binds at the carboxyl end of the parallel strands of the alpha/beta domain. One of the carboxyl groups of the tartrate molecule interacts with the conserved residues Arg-11, His-12, and Arg-15, which form part of the phosphate binding site. Furthermore, the C2 and C3 hydroxyl groups interact with His-257 and Arg-79. The second carboxyl group is close to Arg-79 but makes no direct hydrogen bonds to the protein. A sequence comparison between tartrate-sensitive and -resistant acid phosphatases suggests that these enzymes have different three-dimensional structures.
About this Structure
1RPA is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of rat acid phosphatase in complex with L(+)-tartrate., Lindqvist Y, Schneider G, Vihko P, J Biol Chem. 1993 Oct 5;268(28):20744-6. PMID:8407898
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