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Yorodumi- PDB-1mxh: Crystal Structure of Substrate Complex of Putative Pteridine Redu... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1mxh | ||||||
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Title | Crystal Structure of Substrate Complex of Putative Pteridine Reductase 2 (PTR2) from Trypanosoma cruzi | ||||||
Components | PTERIDINE REDUCTASE 2 | ||||||
Keywords | OXIDOREDUCTASE / SDR TOPOLOGY / PROTEIN-SUBSTRATE COMPLEX | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Trypanosoma cruzi (eukaryote) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.2 Å | ||||||
Authors | Schormann, N. / Pal, B. / Senkovich, O. / Carson, M. / Howard, A. / Smith, C. / Delucas, L. / Chattopadhyay, D. | ||||||
Citation | Journal: J.Struct.Biol. / Year: 2005 Title: Crystal structure of Trypanosoma cruzi pteridine reductase 2 in complex with a substrate and an inhibitor. Authors: Schormann, N. / Pal, B. / Senkovich, O. / Carson, M. / Howard, A. / Smith, C. / Delucas, L. / Chattopadhyay, D. #1: Journal: Acta Crystallogr.,Sect.D / Year: 2001 Title: Expression, purification, crystallization and preliminary crystallographic analysis of recombinant pteridine reductase of Trypanosoma cruzi Authors: Schormann, N. / Pal, B. / Chattopadhyay, D. | ||||||
History |
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Remark 600 | Heterogen Ligand coordinates were taken from PDB entry 1RF7. The coordinate file was missing a ...Heterogen Ligand coordinates were taken from PDB entry 1RF7. The coordinate file was missing a carboxylate group in the glutamate portion. No correction was made since the glutamate portion of ligand DHF shows no clear density in this structure. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1mxh.cif.gz | 209.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1mxh.ent.gz | 169 KB | Display | PDB format |
PDBx/mmJSON format | 1mxh.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mx/1mxh ftp://data.pdbj.org/pub/pdb/validation_reports/mx/1mxh | HTTPS FTP |
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-Related structure data
Related structure data | 1mxfSC S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 29181.277 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Trypanosoma cruzi (eukaryote) / Strain: Sylvio, X10 / Gene: ptr2 / Plasmid: pET15b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)pLysS / References: UniProt: Q8I814 #2: Chemical | ChemComp-NAP / #3: Chemical | ChemComp-DHF / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.3 Å3/Da / Density % sol: 46.7 % | |||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / pH: 6.5 Details: Sodium acetate, cacodylate buffer, pH 6.50, temperature 293K | |||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 293 K / pH: 8 / Method: vapor diffusion, hanging dropDetails: Schormann, N., (2001) Acta Crystallogr.,Sect.D, 57, 1671. | |||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 103 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 17-ID / Wavelength: 0.9537 |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Dec 20, 2000 / Details: MIRRORS |
Radiation | Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9537 Å / Relative weight: 1 |
Reflection | Resolution: 1.77→36 Å / Num. obs: 87817 / % possible obs: 79.8 % / Observed criterion σ(I): 0 / Redundancy: 1.9 % / Biso Wilson estimate: 17.7 Å2 / Rmerge(I) obs: 0.025 / Net I/σ(I): 12.4 |
Reflection | *PLUS Highest resolution: 2.3 Å / Lowest resolution: 50 Å / Num. obs: 47858 / % possible obs: 95.7 % / Redundancy: 2.4 % / Rmerge(I) obs: 0.059 |
Reflection shell | *PLUS Highest resolution: 2.3 Å / Lowest resolution: 2.44 Å / % possible obs: 91.2 % / Redundancy: 1.8 % / Num. unique obs: 7590 / Rmerge(I) obs: 0.182 / Mean I/σ(I) obs: 3.9 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: INHIBITOR COMPLEX SOLVED BY MAD METHOD (PDBID 1MXF) Resolution: 2.2→19.45 Å / Rfactor Rfree error: 0.005 / Data cutoff high absF: 220622 / Data cutoff high rms absF: 220622 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 1 / Stereochemistry target values: ENGH & HUBER
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 52.225 Å2 / ksol: 0.361 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 31.1 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.2→19.45 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.2→2.34 Å / Rfactor Rfree error: 0.014 / Total num. of bins used: 6
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Xplor file |
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Refinement | *PLUS Highest resolution: 2.3 Å / Lowest resolution: 50 Å / Rfactor Rfree: 0.252 / Rfactor Rwork: 0.2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Highest resolution: 2.3 Å / Lowest resolution: 2.44 Å / Rfactor Rfree: 0.288 / Rfactor Rwork: 0.246 |