1P33
Pteridine reductase from Leishmania tarentolae complex with NADPH and MTX
Summary for 1P33
| Entry DOI | 10.2210/pdb1p33/pdb |
| Related | 1E7w 1E92 |
| Descriptor | Pteridine reductase 1, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, METHOTREXATE, ... (4 entities in total) |
| Functional Keywords | pteridine reductase, complex, nadph, mtx, oxidoreductase |
| Biological source | Leishmania tarentolae |
| Total number of polymer chains | 4 |
| Total formula weight | 127890.50 |
| Authors | Zhao, H.,Bray, T.,Ouellette, M.,Zhao, M.,Ferre, R.A.,Matthews, D.,Whiteley, J.M.,Varughese, K.I. (deposition date: 2003-04-16, release date: 2003-09-02, Last modification date: 2023-08-16) |
| Primary citation | Zhao, H.,Bray, T.,Ouellette, M.,Zhao, M.,Ferre, R.A.,Matthews, D.,Whiteley, J.M.,Varughese, K.I. Structure of pteridine reductase (PTR1) from Leishmania tarentolae. Acta Crystallogr.,Sect.D, 59:1539-1544, 2003 Cited by PubMed Abstract: The protozoan parasites Leishmania utilize a pteridine-reducing enzyme, pteridine reductase (PTR1), to bypass antifolate inhibition. The crystal structure of PTR1 from L. tarentolae has been solved as a binary complex with NADPH at 2.8 A resolution. The structure was solved by molecular-replacement techniques using the recently reported L. major PTR1 structure as a search model. Comparisons of the present structure with the L. major PTR1 allowed us to identify regions of flexibility in the molecule. PTR1 is a member of the growing family of short-chain dehydrogenases (SDR) which share the characteristic Tyr(Xaa)(3)Lys motif in the vicinity of the active site. The functional enzyme is a tetramer and the crystallographic asymmetric unit contains a tetramer with 222 point-group symmetry. PubMed: 12925782DOI: 10.1107/S0907444903013131 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.86 Å) |
Structure validation
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