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Yorodumi- PDB-1e7w: One active site, two modes of reduction correlate the mechanism o... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1e7w | ||||||
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Title | One active site, two modes of reduction correlate the mechanism of leishmania pteridine reductase with pterin metabolism and antifolate drug resistance in trpanosomes | ||||||
Components | PTERIDINE REDUCTASE | ||||||
Keywords | OXIDOREDUCTASE / DIHYDROFOLATE REDUCTASE / PTERIDINE REDUCTASE / SHORTCHAIN DEHYDROGENASE / METHOTREXATE RESISTANCE | ||||||
Function / homology | Function and homology information pteridine reductase / 6,7-dihydropteridine reductase activity / pteridine reductase activity / tetrahydrobiopterin biosynthetic process / response to methotrexate / oxidoreductase activity / cytosol Similarity search - Function | ||||||
Biological species | LEISHMANIA MAJOR (eukaryote) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 1.75 Å | ||||||
Authors | Gourley, D.G. / Hunter, W.N. | ||||||
Citation | Journal: Nat.Struct.Biol. / Year: 2001 Title: Pteridine Reductase Mechanism Correlates Pterin Metabolism with Drug Resistance in Trypanosomatid Parasites. Authors: Gourley, D.G. / Schuttelkopf, A. / Leonard, G. / Luba, J. / Hardy, L. / Beverley, S. / Hunter, W.N. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1e7w.cif.gz | 126.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1e7w.ent.gz | 98.1 KB | Display | PDB format |
PDBx/mmJSON format | 1e7w.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1e7w_validation.pdf.gz | 673.6 KB | Display | wwPDB validaton report |
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Full document | 1e7w_full_validation.pdf.gz | 693.8 KB | Display | |
Data in XML | 1e7w_validation.xml.gz | 16 KB | Display | |
Data in CIF | 1e7w_validation.cif.gz | 24.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/e7/1e7w ftp://data.pdbj.org/pub/pdb/validation_reports/e7/1e7w | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.493, 0.87), Vector: Details | BIOMOLECULE | |
-Components
#1: Protein | Mass: 30722.850 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) LEISHMANIA MAJOR (eukaryote) / Strain: CC-1 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): B834 References: UniProt: Q9U1F8, UniProt: Q01782*PLUS, EC: 1.1.1.253 #2: Chemical | #3: Chemical | #4: Chemical | #5: Water | ChemComp-HOH / | Sequence details | EXTRA GLY-SER-HIS SEQUENCE EXTENSION ON N-TERMINAL DISCREPANCIES WITH SEQUENCE IN DATA BASE AS ...EXTRA GLY-SER-HIS SEQUENCE EXTENSION ON N-TERMINAL DISCREPANC | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 2 |
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-Sample preparation
Crystal | Density Matthews: 2.4 Å3/Da / Density % sol: 48.66 % |
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Crystal grow | pH: 5.4 / Details: pH 5.40 |
-Data collection
Diffraction | Mean temperature: 100 K | |||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: SRS / Beamline: PX9.6 / Wavelength: 0.87, 0.886, 0.97950, 0.97960 | |||||||||||||||
Radiation | Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||
Radiation wavelength |
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Reflection | Resolution: 1.75→30 Å / Num. obs: 59475 / % possible obs: 98.2 % / Redundancy: 5.7 % / Biso Wilson estimate: 25.7 Å2 / Rsym value: 0.45 / Net I/σ(I): 24.6 |
-Processing
Software | Name: REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Method to determine structure: MAD / Resolution: 1.75→30 Å / SU B: 2.827 / SU ML: 0.091 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.122 / ESU R Free: 0.127
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Displacement parameters | Biso mean: 32.5 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.75→30 Å
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Refine LS restraints |
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