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Yorodumi- PDB-1xk0: Crystal Structures of the G139A, G139A-NO and G143H Mutants of Hu... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1xk0 | ||||||
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Title | Crystal Structures of the G139A, G139A-NO and G143H Mutants of Human Heme Oxygenase-1 | ||||||
Components | Heme oxygenase 1 | ||||||
Keywords | OXIDOREDUCTASE / heme / heme degredation | ||||||
Function / homology | Function and homology information Regulation of HMOX1 expression and activity / heme oxygenase (biliverdin-producing) / low-density lipoprotein particle clearance / cellular response to cisplatin / heme oxidation / smooth muscle hyperplasia / heme oxygenase (decyclizing) activity / negative regulation of leukocyte migration / wound healing involved in inflammatory response / positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis ...Regulation of HMOX1 expression and activity / heme oxygenase (biliverdin-producing) / low-density lipoprotein particle clearance / cellular response to cisplatin / heme oxidation / smooth muscle hyperplasia / heme oxygenase (decyclizing) activity / negative regulation of leukocyte migration / wound healing involved in inflammatory response / positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis / heme catabolic process / cellular response to arsenic-containing substance / positive regulation of epithelial cell apoptotic process / endothelial cell proliferation / erythrocyte homeostasis / negative regulation of ferroptosis / epithelial cell apoptotic process / Heme degradation / NFE2L2 regulating anti-oxidant/detoxification enzymes / negative regulation of macroautophagy / positive regulation of cell migration involved in sprouting angiogenesis / Insertion of tail-anchored proteins into the endoplasmic reticulum membrane / positive regulation of macroautophagy / The NLRP3 inflammasome / regulation of angiogenesis / Purinergic signaling in leishmaniasis infection / negative regulation of extrinsic apoptotic signaling pathway via death domain receptors / positive regulation of chemokine production / cellular response to cadmium ion / macroautophagy / positive regulation of smooth muscle cell proliferation / negative regulation of smooth muscle cell proliferation / Iron uptake and transport / Heme signaling / response to nicotine / response to hydrogen peroxide / Cytoprotection by HMOX1 / multicellular organismal-level iron ion homeostasis / positive regulation of angiogenesis / cellular response to heat / Interleukin-4 and Interleukin-13 signaling / angiogenesis / positive regulation of canonical NF-kappaB signal transduction / intracellular iron ion homeostasis / response to oxidative stress / mitochondrial outer membrane / intracellular signal transduction / heme binding / endoplasmic reticulum membrane / regulation of transcription by RNA polymerase II / structural molecule activity / perinuclear region of cytoplasm / enzyme binding / endoplasmic reticulum / protein homodimerization activity / extracellular space / nucleoplasm / identical protein binding / membrane / nucleus / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.18 Å | ||||||
Authors | Lad, L. / Koshkin, A. / Ortiz de Montellano, P.R. / Poulos, T.L. | ||||||
Citation | Journal: J.Biol.Inorg.Chem. / Year: 2005 Title: Crystal structures of the G139A, G139A-NO and G143H mutants of human heme oxygenase-1. A finely tuned hydrogen-bonding network controls oxygenase versus peroxidase activity. Authors: Lad, L. / Koshkin, A. / Ortiz de Montellano, P.R. / Poulos, T.L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1xk0.cif.gz | 102.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1xk0.ent.gz | 79.3 KB | Display | PDB format |
PDBx/mmJSON format | 1xk0.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xk/1xk0 ftp://data.pdbj.org/pub/pdb/validation_reports/xk/1xk0 | 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: 26884.562 Da / Num. of mol.: 2 / Mutation: G139A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: HMOX1, HO1, HO / Production host: Escherichia coli (E. coli) References: UniProt: P09601, heme oxygenase (biliverdin-producing) #2: Chemical | #3: Chemical | ChemComp-NO / | #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: 2.01 Å3/Da / Density % sol: 38.79 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: ammonium sulphate, hepes, hexane diol , pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
-Data collection
Diffraction source | Source: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.53 Å |
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Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Jul 7, 2004 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.53 Å / Relative weight: 1 |
Reflection | Resolution: 2.01→50 Å / Num. obs: 29654 / % possible obs: 97.8 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Rsym value: 0.02 |
Reflection shell | Resolution: 2.01→2.18 Å / % possible all: 99 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.18→50 Å / σ(F): 2 /
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Refinement step | Cycle: LAST / Resolution: 2.18→50 Å
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Refine LS restraints | Type: c_bond_d / Dev ideal: 0.006 |