2EFX
The crystal structure of D-amino acid amidase from Ochrobactrum anthropi SV3 complexed with L-phenylalanine amide
Summary for 2EFX
| Entry DOI | 10.2210/pdb2efx/pdb |
| Related | 2efu |
| Descriptor | D-amino acid amidase, BARIUM ION, PHENYLALANINE AMIDE, ... (4 entities in total) |
| Functional Keywords | penicillin recognizing proteins, d-stereospecific amidase, l-phenylalanine amide, hydrolase |
| Biological source | Ochrobactrum anthropi |
| Total number of polymer chains | 6 |
| Total formula weight | 244769.56 |
| Authors | Okazaki, S.,Suzuki, A.,Mizushima, T.,Komeda, H.,Asano, Y.,Yamane, T. (deposition date: 2007-02-26, release date: 2007-03-06, Last modification date: 2023-10-25) |
| Primary citation | Okazaki, S.,Suzuki, A.,Mizushima, T.,Komeda, H.,Asano, Y.,Yamane, T. Structures of D-amino-acid amidase complexed with L-phenylalanine and with L-phenylalanine amide: insight into the D-stereospecificity of D-amino-acid amidase from Ochrobactrum anthropi SV3. Acta Crystallogr.,Sect.D, 64:331-334, 2008 Cited by PubMed Abstract: The crystal structures of D-amino-acid amidase (DAA) from Ochrobactrum anthropi SV3 in complex with L-phenylalanine and with L-phenylalanine amide were determined at 2.3 and 2.2 A resolution, respectively. Comparison of the L-phenylalanine amide complex with the D-phenylalanine complex reveals that the D-stereospecificity of DAA might be achieved as a consequence of three structural factors: (i) the hydrophobic cavity in the region in which the hydrophobic side chain of the substrate is held, (ii) the spatial arrangement of Gln310 O and Glu114 O epsilon2 that fixes the amino N atom of the substrate and (iii) the existence of two cavities that keep the carboxyl/amide group of the substrate near or apart from Ser60 O gamma. PubMed: 18323628DOI: 10.1107/S0907444907067479 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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