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Yorodumi- PDB-1i1l: CRYSTAL STRUCTURE OF ESCHELICHIA COLI BRANCHED-CHAIN AMINO ACID A... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1i1l | ||||||
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Title | CRYSTAL STRUCTURE OF ESCHELICHIA COLI BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE. | ||||||
Components | BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE | ||||||
Keywords | TRANSFERASE / AMINOTRANSFERASE / HEXAMER / PLP / 2-METHYLLEUCINE | ||||||
Function / homology | Function and homology information aspartate biosynthetic process / L-leucine:2-oxoglutarate aminotransferase activity / branched-chain-amino-acid transaminase / L-leucine transaminase activity / L-valine transaminase activity / L-isoleucine transaminase activity / branched-chain amino acid biosynthetic process / branched-chain-amino-acid transaminase activity / L-leucine biosynthetic process / valine biosynthetic process ...aspartate biosynthetic process / L-leucine:2-oxoglutarate aminotransferase activity / branched-chain-amino-acid transaminase / L-leucine transaminase activity / L-valine transaminase activity / L-isoleucine transaminase activity / branched-chain amino acid biosynthetic process / branched-chain-amino-acid transaminase activity / L-leucine biosynthetic process / valine biosynthetic process / isoleucine biosynthetic process / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.4 Å | ||||||
Authors | Okada, K. / Hirotsu, K. / Hayashi, H. / Kagamiyama, H. | ||||||
Citation | Journal: Biochemistry / Year: 2001 Title: Structures of Escherichia coli branched-chain amino acid aminotransferase and its complexes with 4-methylvalerate and 2-methylleucine: induced fit and substrate recognition of the enzyme. Authors: Okada, K. / Hirotsu, K. / Hayashi, H. / Kagamiyama, H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1i1l.cif.gz | 192.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1i1l.ent.gz | 152.5 KB | Display | PDB format |
PDBx/mmJSON format | 1i1l.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/i1/1i1l ftp://data.pdbj.org/pub/pdb/validation_reports/i1/1i1l | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 34131.586 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Production host: Escherichia coli (E. coli) References: UniProt: P00510, UniProt: P0AB80*PLUS, branched-chain-amino-acid transaminase #2: Chemical | #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: 2.72 Å3/Da / Density % sol: 54.73 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: PEG400, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200H / Wavelength: 1.5418 Å |
Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Jan 15, 1997 |
Radiation | Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→40 Å / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 |
Reflection | *PLUS Lowest resolution: 40 Å / Num. obs: 42170 / % possible obs: 98.6 % / Num. measured all: 132437 / Rmerge(I) obs: 0.057 |
Reflection shell | *PLUS Highest resolution: 2.4 Å / Lowest resolution: 2.51 Å / % possible obs: 98.4 % / Rmerge(I) obs: 0.181 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.4→40 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber /
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Refinement step | Cycle: LAST / Resolution: 2.4→40 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Version: 3.851 / Classification: refinement | |||||||||||||||
Refinement | *PLUS Highest resolution: 2.4 Å / Lowest resolution: 40 Å / σ(F): 0 / Rfactor obs: 0.182 | |||||||||||||||
Solvent computation | *PLUS | |||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_deg / Dev ideal: 1.3 | |||||||||||||||
LS refinement shell | *PLUS Rfactor Rfree: 0.283 / Rfactor obs: 0.25 |