1rpa
From Proteopedia
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| , resolution 3.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Acid phosphatase, with EC number 3.1.3.2 | ||||||
| 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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