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Hydrolase(phosphoric monoester) PDB id
1rpa
Jmol
Contents
Protein chain
342 a.a. *
Ligands
NAG-NAG-BMA
NAG
TAR
* Residue conservation analysis
PDB id:
1rpa
Name: Hydrolase(phosphoric monoester)
Title: Three-dimensional structure of rat acid phosphatase in compl l(+) tartrate
Structure: Prostatic acid phosphatase. Chain: a. Engineered: yes
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116
Biol. unit: Dimer (from PQS)
Resolution:
3.00Å     R-factor:   0.215    
Authors: Y.Lindqvist,G.Schneider
Key ref: Y.Lindqvist et al. (1993). Three-dimensional structure of rat acid phosphatase in complex with L(+)-tartrate. J Biol Chem, 268, 20744-20746. PubMed id: 8407898
Date:
12-Jun-93     Release date:   31-May-94    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P20646  (PPAP_RAT) -  Prostatic acid phosphatase
Seq:
Struc: 		381 a.a.
342 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 7 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class 1: E.C.3.1.3.2  - Acid phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: A phosphate monoester + H2O = an alcohol + phosphate
phosphate monoester
 + H(2)O
 = alcohol
 + phosphate
   Enzyme class 2: E.C.3.1.3.5  - 5'-nucleotidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate
5'-ribonucleotide
 + H(2)O
 =
ribonucleoside
Bound ligand (Het Group name = NAG)
matches with 60.00% similarity 		+ phosphate
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   9 terms 
  Biological process     dephosphorylation   1 term 
  Biochemical function     hydrolase activity     4 terms  

 

 
    reference    
 
 
J Biol Chem 268:20744-20746 (1993)
PubMed id: 8407898  
 
 
Three-dimensional structure of rat acid phosphatase in complex with L(+)-tartrate.
Y.Lindqvist, G.Schneider, P.Vihko.
 
  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.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20645695 M.I.Hassan, A.Aijaz, and F.Ahmad (2010).
Structural and functional analysis of human prostatic acid phosphatase.
  Expert Rev Anticancer Ther, 10, 1055-1068.  
19753119 C.K.Ho, A.F.Lam, and L.S.Symington (2009).
Identification of nucleases and phosphatases by direct biochemical screen of the Saccharomyces cerevisiae proteome.
  PLoS One, 4, e6993.  
19836403 H.Singh, R.L.Felts, J.P.Schuermann, T.J.Reilly, and J.J.Tanner (2009).
Crystal Structures of the histidine acid phosphatase from Francisella tularensis provide insight into substrate recognition.
  J Mol Biol, 394, 893-904.
PDB codes: 3it0 3it1 3it2 3it3
17468884 L.Song, Z.Xu, and X.Yu (2007).
Molecular cloning and characterization of a phosphoglycerate mutase gene from Clonorchis sinensis.
  Parasitol Res, 101, 709-714.  
15578709 S.Sharma, P.Pirilä, H.Kaija, K.Porvari, P.Vihko, and A.H.Juffer (2005).
Theoretical investigations of prostatic acid phosphatase.
  Proteins, 58, 295-308.  
15341723 Q.Liu, Q.Huang, X.G.Lei, and Q.Hao (2004).
Crystallographic snapshots of Aspergillus fumigatus phytase, revealing its enzymatic dynamics.
  Structure, 12, 1575-1583.
PDB codes: 1sk8 1sk9 1ska 1skb
10835340 K.Ishikawa, Y.Mihara, K.Gondoh, E.Suzuki, and Y.Asano (2000).
X-ray structures of a novel acid phosphatase from Escherichia blattae and its complex with the transition-state analog molybdate.
  EMBO J, 19, 2412-2423.
PDB codes: 1d2t 1eoi
10027907 H.Kaija, J.Jia, Y.Lindqvist, G.Andersson, and P.Vihko (1999).
Tartrate-resistant bone acid phosphatase: large-scale production and purification of the recombinant enzyme, characterization, and crystallization.
  J Bone Miner Res, 14, 424-430.  
8168503 Y.Lindqvist, G.Schneider, and P.Vihko (1994).
Crystal structures of rat acid phosphatase complexed with the transition-state analogs vanadate and molybdate. Implications for the reaction mechanism.
  Eur J Biochem, 221, 139-142.
PDB code: 1rpt
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.