1daj

COMPARISON OF TERNARY COMPLEXES OF PNEUMOCYSTIS CARINII AND WILD TYPE HUMAN DIHYDROFOLATE REDUCTASE WITH COENZYME NADPH AND A NOVEL CLASSICAL ANTITUMOR FURO[2,3D]PYRIMIDINE ANTIFOLATE

spinqualitylabelsall models 1daj, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1daj is a 1 chain structure with sequence from Pneumocystis carinii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: MOT, NDP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function DYR_PNECA Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also Dihydrofolate reductase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA