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- PDB-1dhf: CRYSTAL STRUCTURES OF RECOMBINANT HUMAN DIHYDROFOLATE REDUCTASE C... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1dhf | ||||||
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Title | CRYSTAL STRUCTURES OF RECOMBINANT HUMAN DIHYDROFOLATE REDUCTASE COMPLEXED WITH FOLATE AND 5-DEAZOFOLATE | ||||||
![]() | DIHYDROFOLATE REDUCTASE![]() | ||||||
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Function / homology | ![]() regulation of removal of superoxide radicals / tetrahydrobiopterin biosynthetic process / Metabolism of folate and pterines / tetrahydrofolate metabolic process / sequence-specific mRNA binding / response to methotrexate / axon regeneration / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Davies /II, J.F. / Kraut, J. | ||||||
![]() | ![]() Title: Crystal structures of recombinant human dihydrofolate reductase complexed with folate and 5-deazafolate. Authors: Davies 2nd., J.F. / Delcamp, T.J. / Prendergast, N.J. / Ashford, V.A. / Freisheim, J.H. / Kraut, J. #1: ![]() Title: Expression and Site-Directed Mutagenesis of Human Dihydrofolate Reductase Authors: Prendergast, N.J. / Delcamp, T.J. / Smith, P.L. / Freisheim, J.H. | ||||||
History |
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Remark 650 | HELIX IN EACH CHAIN, RESIDUES ASP 21 - LEU 22 - PRO 23 - TRP 24 - PRO 25 - PRO 26 ARE IN LEFT- ...HELIX IN EACH CHAIN, RESIDUES ASP 21 - LEU 22 - PRO 23 - TRP 24 - PRO 25 - PRO 26 ARE IN LEFT-HANDED POLYPROLINE HELIX CONFORMATION. | ||||||
Remark 700 | SHEET THE FOLLOWING REMARKS APPLY TO EACH CHAIN. IN THE *HELIX*, *SHEET* AND *TURN* RECORDS BELOW, ...SHEET THE FOLLOWING REMARKS APPLY TO EACH CHAIN. IN THE *HELIX*, *SHEET* AND *TURN* RECORDS BELOW, AN *A* OR *B* HAS BEEN APPENDED TO THE NAMES USED IN THIS REMARK TO DISTINGUISH CHAINS. RESIDUE GLN 102 PARTICIPATES IN BOTH HELIX E AND EP. RESIDUES LYS 108 AND VAL 109 PARTICIPATE IN BOTH HELIX EP AND STRAND E. RESIDUE GLU 172 IS IN TIGHT-TURN 8 AND BETA STRAND G. RESIDUE ILE 175 IS IN TIGHT-TURN 8 AND BETA STRAND H. RESIDUES ASP 110 - MET 111 FORM A BETA-BULGE IN STRAND E. RESIDUES VAL 115 - GLY 116 FORM A BETA-BULGE IN STRAND E. TIGHT TURN 7 DISRUPTS STRAND G. THIS IS REPRESENTED ON THE SHEET RECORDS BELOW BY PRESENTING THE SHEET TWICE WITH STRAND 8 DIFFERENT. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 88.8 KB | Display | ![]() |
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PDB format | ![]() | 68.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Atom site foot note | 1: RESIDUES PRO A 66 AND PRO B 66 ARE CIS PROLINES. 2: IN EACH CHAIN, THE PEPTIDE BOND LINKING GLY 116 TO GLY 117 IS IN THE CIS CONFORMATION. |
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Components
#1: Protein | ![]() Mass: 21349.525 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | ![]() #3: Water | ChemComp-HOH / | ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.34 Å3/Da / Density % sol: 47.36 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow![]() | *PLUS Temperature: 4 ℃ / pH: 5.9 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.3 Å / Num. obs: 16023 / % possible obs: 91 % / Rmerge(I) obs: 0.056 |
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Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Rfactor obs: 0.176 / Highest resolution: 2.3 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.3 Å
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Refine LS restraints |
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Software | *PLUS Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.3 Å / Rfactor obs: 0.176 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |