+Open data
-Basic information
Entry | Database: PDB / ID: 1yiy | ||||||
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Title | Aedes aegypti kynurenine aminotransferase | ||||||
Components | kynurenine aminotransferase; glutamine transaminase K | ||||||
Keywords | TRANSFERASE / kynurenine / kynurenic acid / kynurenine aminotrasferase / Aedes / mosquito / PLP-enzyme / PMP / pyridoxamine phosphate | ||||||
Function / homology | Function and homology information L-kynurenine catabolic process / kynurenine-glyoxylate transaminase activity / kynurenine-glyoxylate transaminase / kynurenine-oxoglutarate transaminase / kynurenine-oxoglutarate transaminase activity / Transferases; Transferring nitrogenous groups; Transaminases / biosynthetic process / pyridoxal phosphate binding / mitochondrion Similarity search - Function | ||||||
Biological species | Aedes aegypti (yellow fever mosquito) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å | ||||||
Authors | Han, Q. / Gao, Y.G. / Robinson, H. / Ding, H. / Wilson, S. / Li, J. | ||||||
Citation | Journal: FEBS J. / Year: 2005 Title: Crystal structures of Aedes aegypti kynurenine aminotransferase. Authors: Han, Q. / Gao, Y.G. / Robinson, H. / Ding, H. / Wilson, S. / Li, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1yiy.cif.gz | 184.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1yiy.ent.gz | 145.7 KB | Display | PDB format |
PDBx/mmJSON format | 1yiy.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1yiy_validation.pdf.gz | 453.9 KB | Display | wwPDB validaton report |
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Full document | 1yiy_full_validation.pdf.gz | 507.5 KB | Display | |
Data in XML | 1yiy_validation.xml.gz | 41.8 KB | Display | |
Data in CIF | 1yiy_validation.cif.gz | 59 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/yi/1yiy ftp://data.pdbj.org/pub/pdb/validation_reports/yi/1yiy | HTTPS FTP |
-Related structure data
Related structure data | 1yizC 1gckS 1v2dS C: citing same article (ref.) S: Starting model for refinement |
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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: 48336.137 Da / Num. of mol.: 2 / Fragment: kynurenine aminotransferase (Residues 49-477) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Aedes aegypti (yellow fever mosquito) / Gene: KAT / Plasmid: PBLUE BAC4.5-BAC-N-BLUE / Production host: Spodoptera frugiperda (fall armyworm) / Strain (production host): sf9 References: UniProt: Q95VY4, UniProt: Q17CS8*PLUS, kynurenine-oxoglutarate transaminase, glutamine-phenylpyruvate transaminase #2: Chemical | ChemComp-BR / #3: Chemical | #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: 2.29 Å3/Da / Density % sol: 46 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: PEG 1000, TRIS.HCl, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
-Data collection
Diffraction | Mean temperature: 123 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X12C / Wavelength: 0.97 Å |
Detector | Type: SIEMENS FOUR-CIRCLE / Detector: DIFFRACTOMETER / Date: Aug 28, 2002 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→10 Å / Num. all: 68715 / Num. obs: 68715 / % possible obs: 97.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 10.4 % / Rmerge(I) obs: 0.063 |
Reflection shell | Resolution: 1.9→1.97 Å / % possible all: 90.5 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1gck, 1v2d Resolution: 1.9→10 Å / Isotropic thermal model: Isotropic / Cross valid method: THROUGHOUT / σ(F): 4 / σ(I): 2 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 20.48 Å2 | |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→10 Å
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Refine LS restraints |
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