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- PDB-1teh: STRUCTURE OF HUMAN LIVER CHICHI ALCOHOL DEHYDROGENASE (A GLUTATHI... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1teh | ||||||
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Title | STRUCTURE OF HUMAN LIVER CHICHI ALCOHOL DEHYDROGENASE (A GLUTATHIONE-DEPENDENT FORMALDEHYDE DEHYDROGENASE) | ||||||
![]() | HUMAN CHICHI ALCOHOL DEHYDROGENASE | ||||||
![]() | OXIDOREDUCTASE / NAD+ DEPENDENT ALCOHOL DEHYDROGENASE GLUTATHIONE DEPENDENT FORMALDEHYDE DEHYDROGENASE | ||||||
Function / homology | ![]() formaldehyde dehydrogenase (NAD+) activity / S-(hydroxymethyl)glutathione dehydrogenase / S-(hydroxymethyl)glutathione dehydrogenase (NADP+) activity / S-(hydroxymethyl)glutathione dehydrogenase (NAD+) activity / fatty acid omega-oxidation / S-(hydroxymethyl)glutathione dehydrogenase [NAD(P)+] activity / formaldehyde catabolic process / response to nitrosative stress / Ethanol oxidation / respiratory system process ...formaldehyde dehydrogenase (NAD+) activity / S-(hydroxymethyl)glutathione dehydrogenase / S-(hydroxymethyl)glutathione dehydrogenase (NADP+) activity / S-(hydroxymethyl)glutathione dehydrogenase (NAD+) activity / fatty acid omega-oxidation / S-(hydroxymethyl)glutathione dehydrogenase [NAD(P)+] activity / formaldehyde catabolic process / response to nitrosative stress / Ethanol oxidation / respiratory system process / 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 / zinc ion binding / extracellular exosome / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Yang, Z.-N. / Hurley, T.D. | ||||||
![]() | ![]() Title: Structure of human chi chi alcohol dehydrogenase: a glutathione-dependent formaldehyde dehydrogenase. Authors: Yang, Z.N. / Bosron, W.F. / Hurley, T.D. #1: ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 151.3 KB | Display | ![]() |
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PDB format | ![]() | 119.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 991.1 KB | Display | ![]() |
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Full document | ![]() | 1015.1 KB | Display | |
Data in XML | ![]() | 31.1 KB | Display | |
Data in CIF | ![]() | 41.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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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Components on special symmetry positions |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.6038, 0.0032, -0.7971), Vector: |
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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) ![]() 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: ![]() |
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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: ![]() |
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 % |
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Processing
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Refinement | Method to determine structure: ![]()
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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: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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