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Yorodumi- PDB-2hhf: X-ray crystal structure of oxidized human mitochondrial branched ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2hhf | ||||||
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Title | X-ray crystal structure of oxidized human mitochondrial branched chain aminotransferase (hBCATm) | ||||||
Components | (Branched-chain-amino-acid aminotransferase, mitochondrial) x 2 | ||||||
Keywords | TRANSFERASE / D-aminoacid aminotransferase-like PLP-dependent enzymes | ||||||
Function / homology | Function and homology information regulation of hormone levels / isoleucine catabolic 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 / Branched-chain amino acid catabolism ...regulation of hormone levels / isoleucine catabolic 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 / Branched-chain amino acid catabolism / L-leucine biosynthetic process / valine biosynthetic process / amino acid biosynthetic process / cellular response to leukemia inhibitory factor / lipid metabolic process / mitochondrial matrix / mitochondrion / nucleoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.8 Å | ||||||
Authors | Yennawar, N.H. / Hutson, S.M. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2006 Title: Human Mitochondrial Branched Chain Aminotransferase Isozyme: STRUCTURAL ROLE OF THE CXXC CENTER IN CATALYSIS. Authors: Yennawar, N.H. / Islam, M.M. / Conway, M. / Wallin, R. / Hutson, S.M. #1: Journal: J.BIOL.CHEM. / Year: 1998 Title: Overexpression and characterization of the human mitochondrial and cytosolic branched-chain aminotransferases. Authors: Davoodi, J. / Drown, P.M. / Bledsoe, R.K. / Wallin, R. / Reinhart, G.D. / Hutson, S.M. #2: Journal: Biochim.Biophys.Acta / Year: 1997 Title: Cloning of the rat and human mitochondrial branched chain aminotransferases (BCATm). Authors: Bledsoe, R.K. / Dawson, P.A. / Hutson, S.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2hhf.cif.gz | 163.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2hhf.ent.gz | 125.9 KB | Display | PDB format |
PDBx/mmJSON format | 2hhf.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2hhf_validation.pdf.gz | 479.1 KB | Display | wwPDB validaton report |
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Full document | 2hhf_full_validation.pdf.gz | 498.5 KB | Display | |
Data in XML | 2hhf_validation.xml.gz | 31.2 KB | Display | |
Data in CIF | 2hhf_validation.cif.gz | 42.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hh/2hhf ftp://data.pdbj.org/pub/pdb/validation_reports/hh/2hhf | HTTPS FTP |
-Related structure data
Related structure data | 2hdkC 2hg8C 2hgwC 2hgxC 1ekfS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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Unit cell |
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-Components
#1: Protein | Mass: 41450.023 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: In this entity, residue 141 in chain A is a modified Tyrosine, TYO. The authors state that Tyrosine 141 has undergone radiation damage in the presence of the oxidizing agent hydrogen peroxide to form TYO. Source: (gene. exp.) Homo sapiens (human) / Gene: BCAT2, BCATM, ECA40 / Plasmid: PET-28A / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21de3 References: UniProt: O15382, branched-chain-amino-acid transaminase | ||||
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#2: Protein | Mass: 41416.012 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: In this entity, residue 641 is TYR. The authors state that the tyrosine of the second monomer (Chain B) is not modified. Source: (gene. exp.) Homo sapiens (human) / Gene: BCAT2, BCATM, ECA40 / Plasmid: PET-28A / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21de3 / References: UniProt: O15382 | ||||
#3: Chemical | #4: Chemical | ChemComp-EPE / | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.09 Å3/Da / Density % sol: 41.17 % |
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Crystal grow | Temperature: 294 K / Method: vapor diffusion, hanging drop / pH: 7 Details: Peg1500, Hepes, pH 7.0, H2O2, VAPOR DIFFUSION, HANGING DROP, temperature 294K |
-Data collection
Diffraction | Mean temperature: 93 K |
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Diffraction source | Source: SYNCHROTRON / Site: CHESS / Beamline: F1 / Wavelength: 0.91609 Å |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Dec 1, 2002 / Details: Si(111) |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.91609 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→30 Å / Num. all: 63136 / Num. obs: 58070 / % possible obs: 92 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Rmerge(I) obs: 0.077 / Χ2: 1.057 / Net I/σ(I): 9 |
Reflection shell | Resolution: 1.8→1.83 Å / Rmerge(I) obs: 0.483 / Num. unique all: 2757 / Χ2: 0.941 / % possible all: 86.9 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB entry 1EKF Resolution: 1.8→30 Å / FOM work R set: 0.79 / σ(F): 2 / Stereochemistry target values: Engh & Huber Details: Due to a feature in the refinement program, the structure was refined with OXT on one or more residues that is not the terminal residue of the sequence. In all these instances the OXT was ...Details: Due to a feature in the refinement program, the structure was refined with OXT on one or more residues that is not the terminal residue of the sequence. In all these instances the OXT was changed to N of the next residue.
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Solvent computation | Bsol: 15.948 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 24.072 Å2
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Refinement step | Cycle: LAST / Resolution: 1.8→30 Å
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Refine LS restraints |
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 50
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Xplor file |
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