1RPA

THREE-DIMENSIONAL STRUCTURE OF RAT ACID PHOSPHATASE IN COMPLEX WITH L(+) TARTRATE

Summary for 1RPA

• Entry DOI: 10.2210/pdb1rpa/pdb
• Descriptor: PROSTATIC ACID PHOSPHATASE, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• Functional Keywords: hydrolase(phosphoric monoester)
• Biological source: Rattus norvegicus (Norway rat)
• Total number of polymer chains: 1
• Total formula weight: 40649.05

Authors

Lindqvist, Y.,Schneider, G. (deposition date: 1993-06-12, release date: 1994-05-31, Last modification date: 2024-11-06)

Primary citation

Lindqvist, Y.,Schneider, G.,Vihko, P.
Three-dimensional structure of rat acid phosphatase in complex with L(+)-tartrate.
J.Biol.Chem., 268:20744-20746, 1993

PubMed Abstract: 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.

PubMed: 8407898

Experimental method

X-RAY DIFFRACTION (3 Å)