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Yorodumi- PDB-1teh: STRUCTURE OF HUMAN LIVER CHICHI ALCOHOL DEHYDROGENASE (A GLUTATHI... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1teh | ||||||
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Title | STRUCTURE OF HUMAN LIVER CHICHI ALCOHOL DEHYDROGENASE (A GLUTATHIONE-DEPENDENT FORMALDEHYDE DEHYDROGENASE) | ||||||
Components | HUMAN CHICHI ALCOHOL DEHYDROGENASE | ||||||
Keywords | OXIDOREDUCTASE / NAD+ DEPENDENT ALCOHOL DEHYDROGENASE GLUTATHIONE DEPENDENT FORMALDEHYDE DEHYDROGENASE | ||||||
Function / homology | Function and homology information formaldehyde dehydrogenase activity / S-(hydroxymethyl)glutathione dehydrogenase / S-(hydroxymethyl)glutathione dehydrogenase (NADP+) activity / S-(hydroxymethyl)glutathione dehydrogenase (NAD+) activity / S-(hydroxymethyl)glutathione dehydrogenase (NAD(P)+) activity / fatty acid omega-oxidation / formaldehyde catabolic process / respiratory system process / response to nitrosative stress / Ethanol oxidation ...formaldehyde dehydrogenase activity / S-(hydroxymethyl)glutathione dehydrogenase / S-(hydroxymethyl)glutathione dehydrogenase (NADP+) activity / S-(hydroxymethyl)glutathione dehydrogenase (NAD+) activity / S-(hydroxymethyl)glutathione dehydrogenase (NAD(P)+) activity / fatty acid omega-oxidation / formaldehyde catabolic process / respiratory system process / response to nitrosative stress / Ethanol oxidation / alcohol dehydrogenase (NAD+) activity, zinc-dependent / : / positive regulation of blood pressure / alcohol dehydrogenase / Oxidoreductases; Acting on the CH-OH group of donors; With NAD+ or NADP+ as acceptor / response to redox state / retinoid metabolic process / fatty acid binding / response to lipopolysaccharide / electron transfer activity / mitochondrion / extracellular exosome / zinc ion binding / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.7 Å | ||||||
Authors | Yang, Z.-N. / Hurley, T.D. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1997 Title: Structure of human chi chi alcohol dehydrogenase: a glutathione-dependent formaldehyde dehydrogenase. Authors: Yang, Z.N. / Bosron, W.F. / Hurley, T.D. #1: Journal: J.Mol.Biol. / Year: 1994 Title: Structures of Three Human Beta Alcohol Dehydrogenase Variants. Correlations with Their Functional Differences Authors: Hurley, T.D. / Bosron, W.F. / Stone, C.L. / Amzel, L.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1teh.cif.gz | 151.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1teh.ent.gz | 119.4 KB | Display | PDB format |
PDBx/mmJSON format | 1teh.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/te/1teh ftp://data.pdbj.org/pub/pdb/validation_reports/te/1teh | HTTPS FTP |
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-Related structure data
Similar structure data |
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-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 on special symmetry positions |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.6038, 0.0032, -0.7971), Vector: |
-Components
#1: Protein | Mass: 39641.000 Da / Num. of mol.: 2 / Source method: isolated from a natural source Details: THE STRUCTURE FOR HOMODIMERIC CHI ALCOHOL DEHYDROGENASE WAS SOLVED WITH ONE NAD+ PER SUBUNIT Source: (natural) Homo sapiens (human) / Organ: LIVER References: UniProt: P11766, alcohol dehydrogenase, EC: 1.2.1.1 #2: Chemical | ChemComp-ZN / #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 2 |
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-Sample preparation
Crystal | Density Matthews: 3.13 Å3/Da / Density % sol: 60 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 8 Details: 15 MG/ML ENZYME IN 280 MM MES, PH 6.7, 2 MM NAD+, 8.0 % PEG8000 AT 295 K, SITTING-DROP METHOD. | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||||||||
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 RUH2R / Wavelength: 1.5418 |
Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Mar 22, 1994 |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→60.7 Å / Num. obs: 24896 / % possible obs: 89.5 % / Observed criterion σ(I): 1 / Redundancy: 4 % / Rmerge(I) obs: 0.095 / Net I/σ(I): 7.8 |
Reflection shell | Resolution: 2.7→2.75 Å / Redundancy: 3.3 % / Rmerge(I) obs: 0.25 / Mean I/σ(I) obs: 2.2 / % possible all: 67 |
Reflection | *PLUS Num. measured all: 97001 |
Reflection shell | *PLUS % possible obs: 67 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.7→8 Å / σ(F): 1
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Displacement parameters | Biso mean: 30.24 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.3 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.7→8 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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