|Entry||Database: PDB / ID: 1ohj|
|Title||HUMAN DIHYDROFOLATE REDUCTASE, MONOCLINIC (P21) CRYSTAL FORM|
|Function / homology|
Function and homology information
G1/S-Specific Transcription / Metabolism of folate and pterines / Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / regulation of removal of superoxide radicals / tetrahydrobiopterin biosynthetic process / tetrahydrofolate metabolic process / methotrexate binding / response to methotrexate / dihydrofolate metabolic process / sequence-specific mRNA binding ...G1/S-Specific Transcription / Metabolism of folate and pterines / Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / regulation of removal of superoxide radicals / tetrahydrobiopterin biosynthetic process / tetrahydrofolate metabolic process / methotrexate binding / response to methotrexate / dihydrofolate metabolic process / sequence-specific mRNA binding / axon regeneration / folic acid metabolic process / folic acid binding / dihydrofolate reductase / dihydrofolate reductase activity / regulation of transcription involved in G1/S transition of mitotic cell cycle / translation repressor activity, mRNA regulatory element binding / tetrahydrofolate biosynthetic process / NADPH binding / one-carbon metabolic process / positive regulation of nitric-oxide synthase activity / negative regulation of translation / drug binding / NADP binding / oxidation-reduction process / mRNA binding / mitochondrion / cytosol
Dihydrofolate reductase / Dihydrofolate reductase (DHFR) domain profile. / Dihydrofolate reductase (DHFR) domain signature. / Dihydrofolate reductase-like domain superfamily / Dihydrofolate reductase conserved site / Dihydrofolate reductase domain
|Biological species||Homo sapiens (human)|
|Method||X-RAY DIFFRACTION / Resolution: 2.5 Å|
|Authors||Cody, V. / Galitsky, N. / Luft, J.R. / Pangborn, W.|
Journal: Biochemistry / Year: 1997
Title: Comparison of two independent crystal structures of human dihydrofolate reductase ternary complexes reduced with nicotinamide adenine dinucleotide phosphate and the very tight-binding inhibitor PT523.
Authors: Cody, V. / Galitsky, N. / Luft, J.R. / Pangborn, W. / Rosowsky, A. / Blakley, R.L.
#1: Journal: J.Biol.Chem. / Year: 1995
Title: Methotrexate-Resistant Variants of Human Dihydrofolate Reductase with Substitutions of Leucine 22. Kinetics, Crystallography, and Potential as Selectable Markers
Authors: Lewis, W.S. / Cody, V. / Galitsky, N. / Luft, J.R. / Pangborn, W. / Chunduru, S.K. / Spencer, H.T. / Appleman, J.R. / Blakley, R.L.
#2: Journal: J.Biol.Chem. / Year: 1994
Title: Methotrexate-Resistant Variants of Human Dihydrofolate Reductase. Effects of Phe31 Substitutions
Authors: Chunduru, S.K. / Cody, V. / Luft, J.R. / Pangborn, W. / Appleman, J.R. / Blakley, R.L.
SummaryFull reportAbout validation report
|Structure viewer||Molecule: |
Downloads & links
A: DIHYDROFOLATE REDUCTASE
|#1: Protein/peptide|| |
Mass: 21349.525 Da / Num. of mol.: 1
Details: COMPLEXED WITH NADPH AND PT523 NA-(4-AMINO-4-DEOXYPTEROYL)-ND-HEMIPHTHALOYL-L-ORNITHINE
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: POTENTIAL / Production host: Escherichia coli (E. coli) / Strain (production host): JM107 / References: UniProt: P00374, dihydrofolate reductase
|#2: Chemical|| ChemComp-NDP / |
|#3: Chemical|| ChemComp-COP / |
|#4: Water|| ChemComp-HOH / |
|Experiment||Method: X-RAY DIFFRACTION|
|Crystal||Density Matthews: 2.54 Å3/Da / Density % sol: 48 %|
*PLUSTemperature: 20 ℃ / pH: 7 / Method: vapor diffusion, hanging drop
|Components of the solutions|
|Radiation||Scattering type: x-ray|
|Radiation wavelength||Relative weight: 1|
|Reflection||Resolution: 2.5→8 Å / Num. obs: 5276 / % possible obs: 93.4 % / Observed criterion σ(I): 2|
|Software||Name: PROFFT / Classification: refinement|
|Refinement||Resolution: 2.5→8 Å|
|Refinement step||Cycle: LAST / Resolution: 2.5→8 Å|
|Refine LS restraints|
Refinement-ID: X-RAY DIFFRACTION
*PLUSRfactor obs: 0.208
*PLUSBiso mean: 16.86 Å2
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