+Open data
-Basic information
Entry | Database: PDB / ID: 1lk9 | |||||||||
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Title | The Three-dimensional Structure of Alliinase from Garlic | |||||||||
Components | ALLIIN LYASEAlliinase | |||||||||
Keywords | LYASE / EGF-like domain / PLP type 1 / chloride binding | |||||||||
Function / homology | Function and homology information alliin lyase / alliin lyase activity / vacuole / chloride ion binding / pyridoxal phosphate binding / protein homodimerization activity Similarity search - Function | |||||||||
Biological species | Allium sativum (garlic) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / SIRAS / Resolution: 1.53 Å | |||||||||
Authors | Kuettner, E.B. / Hilgenfeld, R. / Weiss, M.S. | |||||||||
Citation | Journal: J.Biol.Chem. / Year: 2002 Title: The active principle of garlic at atomic resolution Authors: Kuettner, E.B. / Hilgenfeld, R. / Weiss, M.S. #1: Journal: Arch.Biochem.Biophys. / Year: 2002 Title: PURIFICATION, CHARACTERIZATION AND CRYSTALLIZATION OF ALLIINASE FROM GARLIC Authors: KUETTNER, E.B. / HILGENFELD, R. / WEISS, M.S. #2: Journal: Arch.Biochem.Biophys. / Year: 2002 Title: Erratum to ``Purification, characterization and crystallization of alliinase from garlic. [Arch. Biochem. Biophys. 402, 192-200.]'' Authors: Kuettner, E.B. / Hilgenfeld, R. / Weiss, M.S. | |||||||||
History |
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Remark 600 | heterogen The molecules EPE and DHA are only present at an occupancy of 50%. Their presence is ...heterogen The molecules EPE and DHA are only present at an occupancy of 50%. Their presence is mutually exclusive. | |||||||||
Remark 999 | sequence there are two different sequences in the literature, one contains an Asp in position 176 ...sequence there are two different sequences in the literature, one contains an Asp in position 176 and one contains Asn. The authors have built and refined the structure with an Asp present in this position. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1lk9.cif.gz | 204.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1lk9.ent.gz | 165.3 KB | Display | PDB format |
PDBx/mmJSON format | 1lk9.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lk/1lk9 ftp://data.pdbj.org/pub/pdb/validation_reports/lk/1lk9 | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 51516.477 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: bulb / Source: (natural) Allium sativum (garlic) / References: UniProt: Q01594, alliin lyase |
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-Sugars , 3 types, 4 molecules
#2: Polysaccharide | beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-3)]2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source | ||
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#3: Polysaccharide | Source method: isolated from a genetically manipulated source #4: Polysaccharide | alpha-L-fucopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose | Source method: isolated from a genetically manipulated source |
-Non-polymers , 6 types, 848 molecules
#5: Chemical | ChemComp-SO4 / #6: Chemical | #7: Chemical | #8: Chemical | #9: Chemical | ChemComp-DHA / | #10: 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: 2.49 Å3/Da / Density % sol: 50.6 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.4 Details: PROTEIN: 5 MG/ML ALLIINASE, 5 MM HEPES PH 7.4, 10 % (V/V) GLYCEROL, 0.25 MM PYRIDOXAL-5'-PHOSPHATE, 1 MM S-ETHYL-L-CYSTEINE; PRECIPITANT: 2.9 M AMMONIUM SULFATE, 50 MM HEPES PH 7.4 HANGING ...Details: PROTEIN: 5 MG/ML ALLIINASE, 5 MM HEPES PH 7.4, 10 % (V/V) GLYCEROL, 0.25 MM PYRIDOXAL-5'-PHOSPHATE, 1 MM S-ETHYL-L-CYSTEINE; PRECIPITANT: 2.9 M AMMONIUM SULFATE, 50 MM HEPES PH 7.4 HANGING DROP METHOD(4 MICROL + 4 MICROL), VAPOUR DIFFUSION, VAPOR DIFFUSION, HANGING DROP, temperature 293K | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃Details: Kuettner, E.B., (2002) Arch.Biochem.Biophys., 402, 192. | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: BW7B / Wavelength: 0.8423 Å |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Apr 25, 2000 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.8423 Å / Relative weight: 1 |
Reflection | Resolution: 1.53→12 Å / Num. all: 160747 / Num. obs: 160747 / % possible obs: 98.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 5.8 % / Biso Wilson estimate: 20.7 Å2 / Rmerge(I) obs: 0.055 / Net I/σ(I): 20.3 |
Reflection shell | Resolution: 1.53→1.56 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.508 / Mean I/σ(I) obs: 2.1 / Num. unique all: 8024 / % possible all: 99.9 |
Reflection | *PLUS Lowest resolution: 20 Å / Num. measured all: 928820 / Rmerge(I) obs: 0.057 |
Reflection shell | *PLUS % possible obs: 99.6 % |
-Processing
Software |
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Refinement | Method to determine structure: SIRAS / Resolution: 1.53→12 Å / SU B: 1.52975 / SU ML: 0.05519 / Isotropic thermal model: isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.07531 / ESU R Free: 0.07692 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 25.8 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.53→12 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.53→1.604 Å
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Refinement | *PLUS Lowest resolution: 20 Å / Rfactor Rfree: 0.221 / Rfactor Rwork: 0.193 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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