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- PDB-5ver: MOUSE KYNURENINE AMINOTRANSFERASE III, RE-REFINEMENT OF THE PDB S... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5ver | ||||||
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Title | MOUSE KYNURENINE AMINOTRANSFERASE III, RE-REFINEMENT OF THE PDB STRUCTURE 3E2Z | ||||||
![]() | Kynurenine--oxoglutarate transaminase 3 | ||||||
![]() | TRANSFERASE / AMINOTRANSFERASE III / MOUSE / RE-REFINEMENT | ||||||
Function / homology | ![]() cysteine-S-conjugate beta-lyase activity / L-kynurenine catabolic process / kynurenine-glyoxylate transaminase activity / kynurenine-glyoxylate transaminase / cysteine-S-conjugate beta-lyase / kynurenine-oxoglutarate transaminase / kynurenine-oxoglutarate transaminase activity / kynurenine metabolic process / 2-oxoglutarate metabolic process / amino acid metabolic process ...cysteine-S-conjugate beta-lyase activity / L-kynurenine catabolic process / kynurenine-glyoxylate transaminase activity / kynurenine-glyoxylate transaminase / cysteine-S-conjugate beta-lyase / kynurenine-oxoglutarate transaminase / kynurenine-oxoglutarate transaminase activity / kynurenine metabolic process / 2-oxoglutarate metabolic process / amino acid metabolic process / biosynthetic process / pyridoxal phosphate binding / protein homodimerization activity / mitochondrion / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Wlodawer, A. / Dauter, Z. / Minor, W. / Stanfield, R. / Porebski, P. / Jaskolski, M. / Pozharski, E. / Weichenberger, C.X. / Rupp, B. | ||||||
![]() | Journal: Mol. Cell. Biol. / Year: 2009 Title: Biochemical and structural properties of mouse kynurenine aminotransferase III. Authors: Han, Q. / Robinson, H. / Cai, T. / Tagle, D.A. / Li, J. | ||||||
History |
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Remark 0 | This entry reflects an alternative modeling of the original data in 3E2Z, determined by Zhang, R., ...This entry reflects an alternative modeling of the original data in 3E2Z, determined by Zhang, R., Hatzos, C., Clancy, S., Joachimiak, A. | ||||||
Remark 200 | SEE THE ORIGINAL DATA, ENTRY 3E2Z | ||||||
Remark 280 | SEE THE ORIGINAL DATA, ENTRY 3E2Z |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 174.1 KB | Display | ![]() |
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PDB format | ![]() | 142.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 5vehC ![]() 5vepC ![]() 5veqC ![]() 5vetC ![]() 5vf2C ![]() 5vf5C ![]() 5vgaC C: citing same article ( |
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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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Components on special symmetry positions |
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Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 46224.977 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: Q71RI9, kynurenine-oxoglutarate transaminase, cysteine-S-conjugate beta-lyase, kynurenine-glyoxylate transaminase |
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-Non-polymers , 8 types, 115 molecules ![](data/chem/img/PLP.gif)
![](data/chem/img/EPE.gif)
![](data/chem/img/PGE.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/PMP.gif)
![](data/chem/img/PEG.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/EPE.gif)
![](data/chem/img/PGE.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/PMP.gif)
![](data/chem/img/PEG.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-PLP / | ||||||||||||
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#3: Chemical | #4: Chemical | ChemComp-PGE / | #5: Chemical | ChemComp-GOL / #6: Chemical | ChemComp-CA / #7: Chemical | ChemComp-PMP / | #8: Chemical | ChemComp-PEG / | #9: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.63 Å3/Da / Density % sol: 53.23 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 21% PEG 400, 150 MM CACL2, 10%, GLYCEROL, 100 MM HEPES, PH 7.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Jun 27, 2008 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.0809 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→29.64 Å / Num. obs: 22779 / % possible obs: 95.6 % / Redundancy: 11.9 % / Net I/σ(I): 11.2 |
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Processing
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Refinement | Resolution: 2.81→29.64 Å / SU B: 13.552 / SU ML: 0.264 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.396
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Displacement parameters | Biso mean: 30.46 Å2
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Refinement step | Cycle: LAST / Resolution: 2.81→29.64 Å
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