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Yorodumi- PDB-2w98: CRYSTAL STRUCTURE OF HUMAN ZINC-BINDING ALCOHOL DEHYDROGENASE 1 (... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 2w98 | ||||||
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| Title | CRYSTAL STRUCTURE OF HUMAN ZINC-BINDING ALCOHOL DEHYDROGENASE 1 (ZADH1) IN TERNARY COMPLEX WITH NADP AND PHENYLBUTAZONE | ||||||
Components | PROSTAGLANDIN REDUCTASE 2 | ||||||
Keywords | OXIDOREDUCTASE / 15-OXOPROSTALGLANDIN / MEDIUM-CHAIN DEHYDROGENASE/REDUCTASE | ||||||
| Function / homology | Function and homology information13,14-dehydro-15-oxoprostaglandin 13-reductase / 15-oxoprostaglandin 13-reductase [NAD(P)+] activity / Synthesis of Prostaglandins (PG) and Thromboxanes (TX) / prostaglandin metabolic process / cytoplasm Similarity search - Function | ||||||
| Biological species | HOMO SAPIENS (human) | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.85 Å | ||||||
Authors | Shafqat, N. / Yue, W.W. / Muniz, J. / Picaud, S. / Niesen, F. / Arrowsmith, C. / Weigelt, J. / Edwards, A. / Bountra, C. / Oppermann, U. | ||||||
Citation | Journal: To be PublishedTitle: Crystal Structure of Human Zinc-Binding Alcohol Dehydrogenase 1 Authors: Shafqat, N. / Yue, W.W. / Niesen, F. / Oppermann, U. | ||||||
| History |
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| Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 2w98.cif.gz | 169.1 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb2w98.ent.gz | 133.5 KB | Display | PDB format |
| PDBx/mmJSON format | 2w98.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 2w98_validation.pdf.gz | 3.2 MB | Display | wwPDB validaton report |
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| Full document | 2w98_full_validation.pdf.gz | 3.2 MB | Display | |
| Data in XML | 2w98_validation.xml.gz | 35.8 KB | Display | |
| Data in CIF | 2w98_validation.cif.gz | 50.9 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/w9/2w98 ftp://data.pdbj.org/pub/pdb/validation_reports/w9/2w98 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 2w4qC ![]() 2vnaS C: citing same article ( S: Starting model for refinement |
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| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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| 2 | ![]()
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| Unit cell |
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| Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: 1
NCS ensembles :
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Components
-Protein , 1 types, 2 molecules AB
| #1: Protein | Mass: 39331.707 Da / Num. of mol.: 2 / Fragment: RESIDUES 1-349 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PNIC-CTHF / Production host: ![]() References: UniProt: Q8N8N7, 13,14-dehydro-15-oxoprostaglandin 13-reductase |
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-Non-polymers , 7 types, 510 molecules 












| #2: Chemical | | #3: Chemical | ChemComp-P1Z / #4: Chemical | ChemComp-PO4 / #5: Chemical | ChemComp-LMR / ( | #6: Chemical | ChemComp-CL / | #7: Chemical | ChemComp-NA / | #8: 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: 2.58 Å3/Da / Density % sol: 52.43 % / Description: NONE |
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| Crystal grow | Details: 2.1M NA(MALATE) |
-Data collection
| Diffraction | Mean temperature: 100 K |
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| Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 0.9789 |
| Detector | Type: MARRESEARCH / Detector: CCD / Date: Aug 27, 2008 |
| Radiation | Monochromator: SI (111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.9789 Å / Relative weight: 1 |
| Reflection | Resolution: 1.85→53.37 Å / Num. obs: 66348 / % possible obs: 99.2 % / Observed criterion σ(I): 2 / Redundancy: 2.9 % / Rmerge(I) obs: 0.05 / Net I/σ(I): 13.6 |
| Reflection shell | Resolution: 1.85→1.95 Å / Redundancy: 2.3 % / Rmerge(I) obs: 0.16 / Mean I/σ(I) obs: 5.2 / % possible all: 95.5 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: PDB ENTRY 2VNA Resolution: 1.85→53.4 Å / Cor.coef. Fo:Fc: 0.972 / Cor.coef. Fo:Fc free: 0.967 / SU B: 4.598 / SU ML: 0.071 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.117 / ESU R Free: 0.109 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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| Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso mean: 8.15 Å2
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| Refinement step | Cycle: LAST / Resolution: 1.85→53.4 Å
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| Refine LS restraints |
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