1KP0
The Crystal Structure Analysis of Creatine Amidinohydrolase from Actinobacillus
Summary for 1KP0
| Entry DOI | 10.2210/pdb1kp0/pdb |
| Descriptor | CREATINE AMIDINOHYDROLASE (2 entities in total) |
| Functional Keywords | alpha betal, 3-layer(aba) sandwich, hydrolase |
| Biological source | Actinobacillus |
| Total number of polymer chains | 2 |
| Total formula weight | 89452.68 |
| Authors | Padmanabhan, B.,Paehler, A.,Horikoshi, M. (deposition date: 2001-12-26, release date: 2002-07-31, Last modification date: 2024-10-09) |
| Primary citation | Padmanabhan, B.,Paehler, A.,Horikoshi, M. Structure of creatine amidinohydrolase from Actinobacillus. Acta Crystallogr.,Sect.D, 58:1322-1328, 2002 Cited by PubMed Abstract: 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. PubMed: 12136144DOI: 10.1107/S0907444902010156 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
Download full validation report
