[English] 日本語
Yorodumi- PDB-1aoe: CANDIDA ALBICANS DIHYDROFOLATE REDUCTASE COMPLEXED WITH DIHYDRO-N... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1aoe | ||||||
---|---|---|---|---|---|---|---|
Title | CANDIDA ALBICANS DIHYDROFOLATE REDUCTASE COMPLEXED WITH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (NADPH) AND 1,3-DIAMINO-7-(1-ETHYEPROPYE)-7H-PYRRALO-[3,2-F]QUINAZOLINE (GW345) | ||||||
Components | DIHYDROFOLATE REDUCTASE | ||||||
Keywords | OXIDOREDUCTASE / ANTIFUNGAL TARGET / REDUCTASE | ||||||
Function / homology | Function and homology information dihydrofolate reductase / dihydrofolate reductase activity / tetrahydrofolate biosynthetic process / one-carbon metabolic process / NADP binding Similarity search - Function | ||||||
Biological species | Candida albicans (yeast) | ||||||
Method | X-RAY DIFFRACTION / DIRECT REPLACEMENT / Resolution: 1.6 Å | ||||||
Authors | Whitlow, M. / Howard, A.J. / Stewart, D. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 1997 Title: X-ray crystallographic studies of Candida albicans dihydrofolate reductase. High resolution structures of the holoenzyme and an inhibited ternary complex. Authors: Whitlow, M. / Howard, A.J. / Stewart, D. / Hardman, K.D. / Kuyper, L.F. / Baccanari, D.P. / Fling, M.E. / Tansik, R.L. #1: Journal: J.Med.Chem. / Year: 1996 Title: High-Affinity Inhibitors of Dihydrofolate Reductase: Antimicrobial and Anticancer Activities of 7,8-Dialkyl-1,3-Diaminopyrrolo[3,2-F]Quinazolines with Small Molecular Size Authors: Kuyper, L.F. / Baccanari, D.P. / Jones, M.L. / Hunter, R.N. / Tansik, R.L. / Joyner, S.S. / Boytos, C.M. / Rudolph, S.K. / Knick, V. / Wilson, H.R. / Caddell, J.M. / Friedman, H.S. / Comley, J.C. / Stables, J.N. #2: Journal: J.Biol.Chem. / Year: 1989 Title: Characterization of Candida Albicans Dihydrofolate Reductase Authors: Baccanari, D.P. / Tansik, R.L. / Joyner, S.S. / Fling, M.E. / Smith, P.L. / Freisheim, J.H. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1aoe.cif.gz | 103.2 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1aoe.ent.gz | 79.5 KB | Display | PDB format |
PDBx/mmJSON format | 1aoe.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1aoe_validation.pdf.gz | 660.1 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 1aoe_full_validation.pdf.gz | 677 KB | Display | |
Data in XML | 1aoe_validation.xml.gz | 12.5 KB | Display | |
Data in CIF | 1aoe_validation.cif.gz | 19.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ao/1aoe ftp://data.pdbj.org/pub/pdb/validation_reports/ao/1aoe | HTTPS FTP |
-Related structure data
Related structure data | 1ai9SC 1m78C 1m79C 1m7aC S: Starting model for refinement C: citing same article (ref.) |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
2 |
| ||||||||
Unit cell |
| ||||||||
Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.712, 0.249, 0.656), Vector: |
-Components
#1: Protein | Mass: 22194.527 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Candida albicans (yeast) / Cell line: BL21 / Plasmid: BL21 / Species (production host): Escherichia coli / Cellular location (production host): CYTOPLASM / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: P22906, dihydrofolate reductase #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 2.27 Å3/Da / Density % sol: 43 % | |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | pH: 6.5 Details: A THREE-FOLD EXCESS OF GW345 AND THREE-FOLD EXCESS OF NADPH WAS ADDED TO THE C. ALBICANS DHFR SOLUTION AND LET STAND 277K OVERNIGHT. 17-20 MG/ML C. ALBICANS DHFR IN 50 UM GW345, 50 UM NADPH, ...Details: A THREE-FOLD EXCESS OF GW345 AND THREE-FOLD EXCESS OF NADPH WAS ADDED TO THE C. ALBICANS DHFR SOLUTION AND LET STAND 277K OVERNIGHT. 17-20 MG/ML C. ALBICANS DHFR IN 50 UM GW345, 50 UM NADPH, 20 MM KMES, 1 MM DTT, PH 6.5 WAS MIXED WITH AN EQUAL PART OF 26 - 34% PEG-3350, THE RESERVOIR SOLUTION. | |||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusion, hanging drop | |||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 295 K |
---|---|
Diffraction source | Source: ROTATING ANODE / Type: ELLIOTT GX-21 / Wavelength: 1.5418 |
Detector | Type: SIEMENS / Detector: AREA DETECTOR / Date: Aug 9, 1987 / Details: MONOCHROMATOR |
Radiation | Monochromator: HUBER MONOCHROMATOR / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Highest resolution: 1.6 Å / Num. obs: 45668 / % possible obs: 91.7 % / Observed criterion σ(I): 2 / Redundancy: 3.06 % / Rsym value: 0.0458 |
Reflection shell | Resolution: 1.6→1.7 Å / Redundancy: 1.59 % / Mean I/σ(I) obs: 3.06 / Rsym value: 0.235 / % possible all: 53 |
Reflection | *PLUS Num. measured all: 139612 / Rmerge(I) obs: 0.0458 |
Reflection shell | *PLUS % possible obs: 53 % / Rmerge(I) obs: 0.235 |
-Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: DIRECT REPLACEMENT Starting model: CANDIDA ALBICANS DHFR (PDB ENTRY 1AI9) Resolution: 1.6→10 Å / σ(F): 2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.6→10 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
|