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- PDB-1oyk: Crystal Structures of the Ferric, Ferrous, and Ferrous-NO Forms o... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1oyk | ||||||
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Title | Crystal Structures of the Ferric, Ferrous, and Ferrous-NO Forms of the Asp140Ala Mutant of Human Heme Oxygenase-1: Catalytic Implications | ||||||
![]() | Heme oxygenase 1![]() | ||||||
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Function / homology | ![]() Regulation of HMOX1 expression and activity / heme oxygenase (biliverdin-producing) / low-density lipoprotein particle clearance / cellular response to cisplatin / heme oxidation / smooth muscle hyperplasia / negative regulation of leukocyte migration / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Lad, L. / Wang, J. / Li, H. / Friedman, J. / Ortiz de Montellano, P.R. / Poulos, T.L. | ||||||
![]() | ![]() Title: Crystal structures of the ferric, ferrous, and ferrous-NO forms of the Asp140Ala mutant of human heme oxygenase-1: catalytic implications Authors: Lad, L. / Wang, J. / Li, H. / Friedman, J. / Bhaskar, B. / Ortiz de Montellano, P.R. / Poulos, T.L. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 101.6 KB | Display | ![]() |
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PDB format | ![]() | 78.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1oylC ![]() 1ozeC ![]() 1ozlC ![]() 1ozrC ![]() 1ozwC ![]() 1qq8 C: citing same article ( S: Starting model for refinement |
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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
#1: Protein | ![]() Mass: 26854.605 Da / Num. of mol.: 2 / Fragment: residues 1-233 of SWS P09601 / Mutation: Asp140ala Source method: isolated from a genetically manipulated source Details: Heme-complexed / Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() References: UniProt: P09601, heme oxygenase (biliverdin-producing) #2: Chemical | ![]() #3: Water | ChemComp-HOH / | ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.02 Å3/Da / Density % sol: 39.04 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow![]() | Temperature: 301 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: ammomium sulphate, 1,6 hexane-diol, HEPES, water, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 301K | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.4 / Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 119 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Apr 18, 2002 / Details: mirrors |
Radiation | Monochromator: yale mirrors / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 2.59→50 Å / Num. all: 33028 / Num. obs: 14071 / % possible obs: 98.7 % / Observed criterion σ(I): 2 / Redundancy: 8.1 % / Rmerge(I) obs: 0.071 / Rsym value: 0.066 / Net I/σ(I): 19.8 |
Reflection | *PLUS Num. obs: 33028 / Num. measured all: 135214 / Rmerge(I) obs: 0.066 |
Reflection shell | *PLUS Rmerge(I) obs: 0.532 / Mean I/σ(I) obs: 2.01 |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: 1QQ8 ![]() 1qq8 Resolution: 2.59→50 Å / Isotropic thermal model: isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.59→50 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: 10
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Refinement | *PLUS % reflection Rfree: 5 % / Rfactor Rfree![]() ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |