3HMK
Crystal Structure of Serine Racemase
Summary for 3HMK
| Entry DOI | 10.2210/pdb3hmk/pdb |
| Related | 1v71 1wtc 3FKP 3fda |
| Descriptor | Serine racemase, MANGANESE (II) ION, PYRIDOXAL-5'-PHOSPHATE, ... (4 entities in total) |
| Functional Keywords | serine racemase, d-serine, pyridoxal phosphate, plp, nmda glutamate receptor, schizophrenia, isomerase |
| Biological source | Rattus norvegicus (rat) |
| Total number of polymer chains | 2 |
| Total formula weight | 73763.57 |
| Authors | Smith, M.A.,Barker, J.,Mack, V.,Ebneth, A.,Felicetti, B.,Woods, M. (deposition date: 2009-05-29, release date: 2010-01-26, Last modification date: 2023-11-01) |
| Primary citation | Smith, M.A.,Mack, V.,Ebneth, A.,Moraes, I.,Felicetti, B.,Wood, M.,Schonfeld, D.,Mather, O.,Cesura, A.,Barker, J. The structure of mammalian serine racemase: evidence for conformational changes upon inhibitor binding. J.Biol.Chem., 285:12873-12881, 2010 Cited by PubMed Abstract: Serine racemase is responsible for the synthesis of D-serine, an endogenous co-agonist for N-methyl-D-aspartate receptor-type glutamate receptors (NMDARs). This pyridoxal 5'-phosphate-dependent enzyme is involved both in the reversible conversion of L- to D-serine and serine catabolism by alpha,beta-elimination of water, thereby regulating D-serine levels. Because D-serine affects NMDAR signaling throughout the brain, serine racemase is a promising target for the treatment of disorders related to NMDAR dysfunction. To provide a molecular basis for rational drug design the x-ray crystal structures of human and rat serine racemase were determined at 1.5- and 2.1-A resolution, respectively, and in the presence and absence of the orthosteric inhibitor malonate. The structures revealed a fold typical of beta-family pyridoxal 5'-phosphate enzymes, with both a large domain and a flexible small domain associated into a symmetric dimer, and indicated a ligand-induced rearrangement of the small domain that organizes the active site for specific turnover of the substrate. PubMed: 20106978DOI: 10.1074/jbc.M109.050062 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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