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Open data
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Basic information
Entry | Database: PDB / ID: 1cxp | |||||||||
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Title | CRYOGENIC CRYSTAL STRUCTURE OF HUMAN MYELOPEROXIDASE ISOFORM C | |||||||||
![]() | (MYELOPEROXIDASE![]() | |||||||||
![]() | ![]() ![]() | |||||||||
Function / homology | ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() | |||||||||
![]() | Fiedler, T.J. / Fenna, R.E. | |||||||||
![]() | ![]() Title: X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution. Authors: Fiedler, T.J. / Davey, C.A. / Fenna, R.E. #1: ![]() Title: Structure of the Green Heme in Myeloperoxidase Authors: Fenna, R. / Zeng, J. / Davey, C. #2: ![]() Title: 2.3 Angstrom Resolution X-Ray Crystal Structure of the Bisubstrate Analogue Inhibitor Salicylhydroxamic Acid Bound to Human Myeloperoxidase: A Model for a Prereaction Complex with Hydrogen Peroxide Authors: Davey, C.A. / Fenna, R.E. #3: ![]() Title: X-Ray Crystal Structure of Canine Myeloperoxidase at 3 Angstrom Resolution Authors: Zeng, J. / Fenna, R.E. #4: ![]() Title: Site-Directed Mutagenesis of Human Myeloperoxidase: Further Identification of Residues Involved in Catalytic Activity and Heme Interaction Authors: Jacquet, A. / Garcia-Quintana, L. / Deleersnyder, V. / Fenna, R. / Bollen, A. / Moguilevsky, N. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 258.7 KB | Display | ![]() |
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PDB format | ![]() | 209.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related 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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3 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.60975, 0.67889, -0.40903), Vector ![]() |
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Components
-Protein , 2 types, 4 molecules ABCD
#1: Protein | ![]() Mass: 11903.343 Da / Num. of mol.: 2 / Fragment: LIGHT CHAIN / Source method: isolated from a natural source / Source: (natural) ![]() ![]() ![]() ![]() #2: Protein | ![]() Mass: 53234.191 Da / Num. of mol.: 2 / Fragment: HEAVY CHAIN / Source method: isolated from a natural source / Source: (natural) ![]() ![]() ![]() ![]() |
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-Sugars , 2 types, 6 molecules ![](data/chem/img/NAG.gif)
#3: Polysaccharide | ![]() Source method: isolated from a genetically manipulated source #7: Sugar | ChemComp-NAG / ![]() |
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-Non-polymers , 6 types, 853 molecules ![](data/chem/img/CL.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/HEM.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/ACT.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/HEM.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/ACT.gif)
![](data/chem/img/HOH.gif)
#4: Chemical | ![]() #5: Chemical | ![]() #6: Chemical | ![]() #8: Chemical | #9: Chemical | ChemComp-ACT / ![]() #10: Water | ChemComp-HOH / | ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.47 Å3/Da / Density % sol: 50.14 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow![]() | Method: vapor diffusion, hanging drop / pH: 5.5 Details: POLYETHYLENE GLYCOL 8000, AMMONIUM SULFATE, SODIUM ACETATE, CALCIUM CHLORIDE, pH 5.50, VAPOR DIFFUSION, HANGING DROP | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 5.5 | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 85 K |
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Diffraction source | Source: ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: May 13, 1997 / Details: LONG FOCUSING MIRRORS, ADSC |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 1.75→50 Å / Num. obs: 128125 / % possible obs: 99.8 % / Observed criterion σ(I): 0 / Redundancy: 4.1 % / Biso Wilson estimate: 16.82 Å2 / Rmerge(I) obs: 0.053 / Net I/σ(I): 12.6 |
Reflection shell | Resolution: 1.75→1.81 Å / Redundancy: 3.9 % / Rmerge(I) obs: 0.22 / Mean I/σ(I) obs: 5.92 / % possible all: 99.4 |
Reflection | *PLUS Highest resolution: 1.75 Å / Lowest resolution: 50 Å / Observed criterion σ(I): 0 / Redundancy: 4.1 % / Num. measured all: 525526 |
Reflection shell | *PLUS % possible obs: 99.4 % / Redundancy: 3.9 % / Rmerge(I) obs: 0.22 / Mean I/σ(I) obs: 5.92 |
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Processing
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Refinement | Resolution: 1.8→30 Å / σ(F): 2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.8→30 Å
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Refine LS restraints |
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Refine LS restraints NCS | NCS model details: MATRIX 1 RELATES CHAIN A TO CHAIN B | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 1.8→1.86 Å / Total num. of bins used: 10
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | *PLUS Rfactor Rfree: 0.292 / Rfactor Rwork: 0.266 / Rfactor obs: 0.266 |