1kp0 | pdb_00001kp0

The Crystal Structure Analysis of Creatine Amidinohydrolase from Actinobacillus

spinqualitylabelsall models 1kp0, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1kp0 is a 2 chain structure with sequence from Actinobacillus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: ASX, GLX Activity: Creatinase, with EC number 3.5.3.3 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The crystal structure of Actinobacillus creatine amidinohydrolase has been solved by molecular replacement. The amino-acid sequence has been derived from the crystal structure. Crystals belong to space group I222, with unit-cell parameters a = 111.26 (3), b = 113.62 (4), c = 191.65 (2) A, and contain two molecules in an asymmetric unit. The structure was refined to an R factor of 18.8% at 2.7 A resolution. The crystal structure contains a dimer of 402 residues and 118 water molecules. The protein structure is bilobal, consisting of a small N-terminal domain and a large C-terminal domain. The C-terminal domain has a pitta-bread fold, similar to that found in Pseudomonas putida creatinase, proline aminopeptidases and methionine aminopeptidase. Comparison with complex crystal structures of P. putida creatinase reveals that the enzyme activity of Actinobacillus creatinase might be similar to that of P. putida creatinase. Structure of creatine amidinohydrolase from Actinobacillus.,Padmanabhan B, Paehler A, Horikoshi M Acta Crystallogr D Biol Crystallogr. 2002 Aug;58(Pt 8):1322-8. Epub 2002, Jul 20. PMID:12136144 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA