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Open data
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Basic information
Entry | Database: PDB / ID: 2ch1 | ||||||
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Title | Structure of Anopheles gambiae 3-hydroxykynurenine transaminase | ||||||
![]() | 3-HYDROXYKYNURENINE TRANSAMINASE | ||||||
![]() | TRANSFERASE / PLP-ENZYME / KYNURENINE PATHWAY / ANOPHELES GAMBIAE / 3-HYDROXYKYNURENINE TRANSAMINASE | ||||||
Function / homology | ![]() : / alanine-glyoxylate transaminase / L-kynurenine catabolic process / kynurenine-glyoxylate transaminase activity / kynurenine-glyoxylate transaminase / glycine biosynthetic process, by transamination of glyoxylate / serine-pyruvate transaminase activity / alanine-glyoxylate transaminase activity / glyoxylate catabolic process / peroxisome / pyridoxal phosphate binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Rossi, F. / Garavaglia, S. / Giovenzana, G.B. / Arca, B. / Li, J. / Rizzi, M. | ||||||
![]() | ![]() Title: Crystal Structure of the Anopheles Gambiae 3-Hydroxykynurenine Transaminase Authors: Rossi, F. / Garavaglia, S. / Giovenzana, G.B. / Arca, B. / Li, J. / Rizzi, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 310.5 KB | Display | ![]() |
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PDB format | ![]() | 253.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 424.9 KB | Display | ![]() |
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Full document | ![]() | 457.4 KB | Display | |
Data in XML | ![]() | 35 KB | Display | |
Data in CIF | ![]() | 52.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2ch2C ![]() 1h0cS 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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1 | ![]()
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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 / Ens-ID: 1 / Beg auth comp-ID: LYS / Beg label comp-ID: LYS / End auth comp-ID: PHE / End label comp-ID: PHE / Refine code: 1 / Auth seq-ID: 2 - 389 / Label seq-ID: 2 - 389
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Components
#1: Protein | Mass: 44350.094 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: GASUA / Plasmid: PET16B / Production host: ![]() ![]() #2: Chemical | ChemComp-PLP / #3: Chemical | ChemComp-GOL / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.43 Å3/Da / Density % sol: 50 % |
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Crystal grow | pH: 7 / Details: pH 7.00 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: Feb 13, 2005 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→20 Å / Num. obs: 65686 / % possible obs: 98.9 % / Observed criterion σ(I): 0 / Redundancy: 3.1 % / Rmerge(I) obs: 0.06 / Net I/σ(I): 13.2 |
Reflection shell | Resolution: 2.2→2.4 Å / Redundancy: 2.9 % / Rmerge(I) obs: 0.1 / Mean I/σ(I) obs: 3.2 / % possible all: 98.5 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1H0C Resolution: 2.4→50 Å / Cor.coef. Fo:Fc: 0.938 / Cor.coef. Fo:Fc free: 0.924 / SU B: 9.038 / SU ML: 0.207 / Cross valid method: THROUGHOUT / ESU R: 0.482 / ESU R Free: 0.262 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. RESIDUES 1 AND 390-396 WERE NOT VISIBLE IN THE ELECTRON DENSITY AND NOT INCLUDED IN THE FINAL MODEL
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 40.69 Å2
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Refinement step | Cycle: LAST / Resolution: 2.4→50 Å
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Refine LS restraints |
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