+Open data
-Basic information
Entry | Database: PDB / ID: 1dgh | ||||||
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Title | HUMAN ERYTHROCYTE CATALASE 3-AMINO-1,2,4-TRIAZOLE COMPLEX | ||||||
Components | (PROTEIN (CATALASE)) x 2 | ||||||
Keywords | OXIDOREDUCTASE / CATALASE / HEME / NADPH / HYDROGEN PEROXIDE / 3-AMINO-1 / 2 / 4-TRIAZOLE / INHIBITOR | ||||||
Function / homology | Function and homology information response to phenylpropanoid / aminoacylase activity / catalase complex / hemoglobin metabolic process / response to inactivity / cellular detoxification of hydrogen peroxide / response to light intensity / response to L-ascorbic acid / response to ozone / oxidoreductase activity, acting on peroxide as acceptor ...response to phenylpropanoid / aminoacylase activity / catalase complex / hemoglobin metabolic process / response to inactivity / cellular detoxification of hydrogen peroxide / response to light intensity / response to L-ascorbic acid / response to ozone / oxidoreductase activity, acting on peroxide as acceptor / catalase / UV protection / response to fatty acid / response to vitamin A / catalase activity / triglyceride metabolic process / peroxisomal membrane / ureteric bud development / antioxidant activity / Detoxification of Reactive Oxygen Species / peroxisomal matrix / positive regulation of cell division / response to hyperoxia / response to vitamin E / FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes / response to cadmium ion / aerobic respiration / cholesterol metabolic process / response to reactive oxygen species / response to activity / hydrogen peroxide catabolic process / Peroxisomal protein import / response to lead ion / response to insulin / response to hydrogen peroxide / cellular response to growth factor stimulus / osteoblast differentiation / peroxisome / response to estradiol / NADP binding / response to ethanol / secretory granule lumen / ficolin-1-rich granule lumen / response to hypoxia / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / response to xenobiotic stimulus / focal adhesion / intracellular membrane-bounded organelle / heme binding / Neutrophil degranulation / negative regulation of apoptotic process / enzyme binding / protein homodimerization activity / protein-containing complex / mitochondrion / extracellular exosome / extracellular region / membrane / identical protein binding / metal ion binding / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å | ||||||
Authors | Putnam, C.D. / Arvai, A.S. / Bourne, Y. / Tainer, J.A. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2000 Title: Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanism. Authors: Putnam, C.D. / Arvai, A.S. / Bourne, Y. / Tainer, J.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1dgh.cif.gz | 432.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1dgh.ent.gz | 349.9 KB | Display | PDB format |
PDBx/mmJSON format | 1dgh.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/dg/1dgh ftp://data.pdbj.org/pub/pdb/validation_reports/dg/1dgh | HTTPS FTP |
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-Related structure data
Related structure data | 1dgbC 1dgfSC 1dggC C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 56713.438 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell: ERYTHROCYTE / References: UniProt: P04040, catalase #2: Protein | Mass: 56794.492 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell: ERYTHROCYTE / References: UniProt: P04040, catalase #3: Chemical | ChemComp-HEM / #4: Chemical | #5: 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: 3.01 Å3/Da / Density % sol: 59.12 % | ||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion / pH: 8 Details: 6.5 - 8.0% PEG4000, PROTEIN AT 40 MG/ML IN 50MM TRISCL, PH 8.0, VAPOR DIFFUSION, temperature 298K | ||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 200 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRL / Beamline: BL7-1 / Wavelength: 1.08 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Mar 6, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.08 Å / Relative weight: 1 |
Reflection | Resolution: 2→30 Å / Num. all: 173373 / Num. obs: 173373 / % possible obs: 93.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 2.6 % / Biso Wilson estimate: 7.925 Å2 / Rsym value: 0.047 / Net I/σ(I): 17.3 |
Reflection shell | Resolution: 2→2.07 Å / Redundancy: 2.6 % / Mean I/σ(I) obs: 5.2 / Rsym value: 0.156 / % possible all: 92.8 |
Reflection | *PLUS Num. measured all: 449780 / Rmerge(I) obs: 0.047 |
Reflection shell | *PLUS % possible obs: 92.8 % / Rmerge(I) obs: 0.156 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1DGF Resolution: 2→20 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: ENGH & HUBER Details: BOND ANGLES AND LENGTHS TO THE HEME IRON FROM BOTH THE TYR358 LIGAND AND THE HEME NITROGENS WERE UNCONSTRAINED
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Displacement parameters | Biso mean: 39.79 Å2
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Refinement step | Cycle: LAST / Resolution: 2→20 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Version: 3.851 / Classification: refinement | ||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||
Displacement parameters | *PLUS |