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Open data
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Basic information
Entry | Database: PDB / ID: 1llp | |||||||||
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Title | LIGNIN PEROXIDASE (ISOZYME H2) PI 4.15 | |||||||||
![]() | LIGNIN PEROXIDASE | |||||||||
![]() | OXIDOREDUCTASE / HEME PROTEIN / GLYCO PROTEIN | |||||||||
Function / homology | ![]() lignin peroxidase / diarylpropane peroxidase activity / lignin catabolic process / response to reactive oxygen species / hydrogen peroxide catabolic process / cellular response to oxidative stress / heme binding / metal ion binding Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Choinowski, T.H. / Piontek, K. / Glumoff, T. | |||||||||
![]() | ![]() Title: The crystal structure of lignin peroxidase at 1.70 A resolution reveals a hydroxy group on the cbeta of tryptophan 171: a novel radical site formed during the redox cycle. Authors: Choinowski, T. / Blodig, W. / Winterhalter, K.H. / Piontek, K. #1: ![]() Title: Do Carbohydrates Play a Role in the Lignin Peroxidase Cycle? Redox Catalysis in the Endergonic Region of the Driving Force Authors: Schoemaker, H.E. / Lundell, T.K. / Floris, R. / Glumoff, T. / Winterhalter, K.H. / Piontek, K. #2: ![]() Title: The Oxidation of Veratryl Alcohol, Dimeric Lignin Models and Lignin by Lignin Peroxidase: The Redox Cycle Revisited Authors: Schoemaker, H.E. / Lundell, T.K. / Hatakka, A.I. / Piontek, K. #3: ![]() Title: Low Ph Crystal Structure of Glycosylated Lignin Peroxidase from Phanerochaete Chrysosporium at 2.5 Angstrom Resolution Authors: Piontek, K. / Glumoff, T. / Winterhalter, K. | |||||||||
History |
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Remark 700 | SHEET SHEET SHEET_ID: A; DETERMINATION METHOD: DSSP; SHORT ANTIPARALLEL BETA-SHEET. SHEET_ID: B; ...SHEET SHEET SHEET_ID: A; DETERMINATION METHOD: DSSP; SHORT ANTIPARALLEL BETA-SHEET. SHEET_ID: B; SHORT ANTIPARALLEL BETA-SHEET. SHEET_ID: C; SHORT ANTIPARALLEL BETA-SHEET. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 86.1 KB | Display | ![]() |
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PDB format | ![]() | 66.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 20.4 KB | Display | |
Data in CIF | ![]() | 30.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 36411.648 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: P49012, Oxidoreductases; Acting on a peroxide as acceptor; Peroxidases |
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-Sugars , 3 types, 3 molecules ![](data/chem/img/MAN.gif)
![](data/chem/img/A2G.gif)
![](data/chem/img/A2G.gif)
#2: Polysaccharide | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source |
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#3: Sugar | ChemComp-MAN / |
#4: Sugar | ChemComp-A2G / |
-Non-polymers , 4 types, 374 molecules ![](data/chem/img/CA.gif)
![](data/chem/img/OH.gif)
![](data/chem/img/HEM.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/OH.gif)
![](data/chem/img/HEM.gif)
![](data/chem/img/HOH.gif)
#5: Chemical | #6: Chemical | ChemComp-OH / | #7: Chemical | ChemComp-HEM / | #8: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.31 Å3/Da / Density % sol: 62.83 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 4 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 277 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Nov 17, 1993 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.92 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→10 Å / Num. obs: 52732 / % possible obs: 98.3 % / Observed criterion σ(I): 0 / Redundancy: 5 % / Rmerge(I) obs: 0.083 |
Reflection | *PLUS Num. measured all: 243426 / Rmerge(I) obs: 0.083 |
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Processing
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Refinement | Resolution: 1.7→10 Å / σ(F): 2
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Displacement parameters | Biso mean: 16.62 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.15 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.7→10 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Num. reflection obs: 52504 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 13.6 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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