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- PDB-1dr4: CRYSTAL STRUCTURES OF ORGANOMERCURIAL-ACTIVATED CHICKEN LIVER DIH... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1dr4 | ||||||
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Title | CRYSTAL STRUCTURES OF ORGANOMERCURIAL-ACTIVATED CHICKEN LIVER DIHYDROFOLATE REDUCTASE COMPLEXES | ||||||
![]() | DIHYDROFOLATE REDUCTASE | ||||||
![]() | OXIDOREDUCTASE | ||||||
Function / homology | ![]() tetrahydrofolate metabolic process / response to methotrexate / dihydrofolate metabolic process / glycine biosynthetic process / dihydrofolate reductase / dihydrofolate reductase activity / folic acid metabolic process / tetrahydrofolate biosynthetic process / one-carbon metabolic process / NADP binding ...tetrahydrofolate metabolic process / response to methotrexate / dihydrofolate metabolic process / glycine biosynthetic process / dihydrofolate reductase / dihydrofolate reductase activity / folic acid metabolic process / tetrahydrofolate biosynthetic process / one-carbon metabolic process / NADP binding / mRNA binding / mitochondrion Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Mctigue, M.A. / Davies /II, J.F. / Kaufman, B.T. / Xuong, N.-H. / Kraut, J. | ||||||
![]() | ![]() Title: Crystal Structures of Organomercurial-Activated Chicken Liver Dihydrofolate Reductase Complexes Authors: Mctigue, M.A. / Davies II, J.F. / Kaufman, B.T. / Xuong, N.-H. / Kraut, J. #1: ![]() Title: Crystal Structures of Recombinant Human Dihydrofolate Reductase Complexed with Folate and 5-Deazafolate Authors: Davies II, J.F. / Delcamp, T.J. / Prendergast, N.J. / Ashford, V.A. / Freisheim, J.H. / Kraut, J. #2: ![]() Title: Refined Crystal Structure of Escherichia Coli and Chicken Liver Dihydrofolate Reductase Containing Bound Trimethoprim Authors: Matthews, D.A. / Bolin, J.T. / Burridge, J.M. / Filman, D.J. / Volz, K.W. / Kaufman, B.T. / Beddell, C.R. / Champness, J.N. / Stammers, D.K. / Kraut, J. #3: ![]() Title: Dihydrofolate Reductase, the Stereochemistry of Inhibitor Selectivity Authors: Matthews, D.A. / Bolin, J.T. / Burridge, J.M. / Filman, D.J. / Volz, K.W. / Kraut, J. #4: ![]() Title: Crystal Structure of Avian Dihydrofolate Reductase Containing Phenyltriazine and Nadph Authors: Volz, K.W. / Matthews, D.A. / Alden, R.A. / Freer, S.T. / Hansch, C. / Kaufman, B.T. / Kraut, J. #5: ![]() Title: Primary Structure of Chicken Liver Dihydrofolate Reductase Authors: Kumar, A.A. / Blankenship, D.T. / Kaufman, B.T. / Freisheim, J.H. | ||||||
History |
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Remark 650 | HELIX RESIDUES 21-26 (NLPWPP) FORM LEFT-HANDED POLYPROLINE HELIX. RESIDUES 108 AND 109 PARTICIPATE ...HELIX RESIDUES 21-26 (NLPWPP) FORM LEFT-HANDED POLYPROLINE HELIX. RESIDUES 108 AND 109 PARTICIPATE IN BOTH HELIX EP AND BETA STRAND E. | ||||||
Remark 700 | SHEET RESIDUES 110 AND 111 FORM A BETA-BULGE IN STRAND E. RESIDUES 115 AND 116 FORM A BETA-BULGE IN ...SHEET RESIDUES 110 AND 111 FORM A BETA-BULGE IN STRAND E. RESIDUES 115 AND 116 FORM A BETA-BULGE IN STRAND E. TIGHT TURN 7 (RESIDUES 162-165) DISRUPT LAST STRAND OF SHEET INTO 2 STRANDS 8 AND 9. THIS STRAND IS CONTINUOUS IN E. COLI. A BETA BULGE IS PRESENT HERE IN L. CASEI. RESIDUES 172 AND 175 PARTICIPATE IN BOTH TIGHT-TURN 8 AND BETA STRANDS 7 AND 9. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 56.5 KB | Display | ![]() |
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PDB format | ![]() | 39.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 485.9 KB | Display | ![]() |
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Full document | ![]() | 499.5 KB | Display | |
Data in XML | ![]() | 8.2 KB | Display | |
Data in CIF | ![]() | 11.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 |
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2 | ![]()
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Unit cell |
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Atom site foot note | 1: SEE REMARK 6. 2: RESIDUES 21-26 (NLPWPP) FORM LEFT-HANDED POLYPROLINE HELIX. 3: CIS PROLINE - PRO 66 4: RESIDUES 108 AND 109 PARTICIPATE IN BOTH HELIX EP AND BETA STRAND E. 5: RESIDUES 110 AND 111 FORM A BETA-BULGE IN STRAND E. / 6: RESIDUES 115 AND 116 FORM A BETA-BULGE IN STRAND E. 7: PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION GLY 116 - GLY 117 6.474 8: TIGHT TURN 7 (RESIDUES 162-165) DISRUPT LAST STRAND OF SHEET INTO 2 STRANDS 8 AND 9. THIS STRAND IS CONTINUOUS IN E. COLI. A BETA BULGE IS PRESENT HERE IN L. CASEI. 9: RESIDUES 172 AND 175 PARTICIPATE IN BOTH TIGHT-TURN 8 AND BETA STRANDS 7 AND 9. 10: RESIDUE 200 (CALCIUM ION) LIES ON THE CRYSTALLOGRAPHIC TWO-FOLD AT ONE-HALF OCCUPANCY. | ||||||||
Components on special symmetry positions |
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Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 21679.932 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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-Non-polymers , 5 types, 80 molecules ![](data/chem/img/HG.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/NAP.gif)
![](data/chem/img/HBI.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/NAP.gif)
![](data/chem/img/HBI.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-HG / |
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#3: Chemical | ChemComp-CA / |
#4: Chemical | ChemComp-NAP / |
#5: Chemical | ChemComp-HBI / |
#6: Water | ChemComp-HOH / |
-Details
Compound details | CYSTEINE 11 HAS A MERCURY ATOM COVALENTLY BOUND TO SG IN TWO CONFORMATIONS. THE METHYL GROUP BOUND ...CYSTEINE 11 HAS A MERCURY ATOM COVALENTLY |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.62 Å3/Da / Density % sol: 53.03 % | ||||||||
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Crystal grow | *PLUS pH: 5.5 / Method: other | ||||||||
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 |
Reflection shell | *PLUS Highest resolution: 2 Å / Lowest resolution: 2.05 Å |
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Processing
Software | Name: PROLSQ / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Rfactor obs: 0.15 / Highest resolution: 2.4 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.4 Å
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