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Yorodumi- PDB-1scq: K236L mutant of hydroxynitrile lyase from Hevea brasiliensis in c... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1scq | ||||||
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Title | K236L mutant of hydroxynitrile lyase from Hevea brasiliensis in complex with acetonecyanohydrin | ||||||
Components | (S)-acetone-cyanohydrin lyase | ||||||
Keywords | LYASE / alpha-beta hydrolase fold / substrate complex / catalytic triad | ||||||
Function / homology | Function and homology information (S)-hydroxynitrile lyase / aliphatic (S)-hydroxynitrile lyase activity / aromatic (S)-hydroxynitrile lyase activity Similarity search - Function | ||||||
Biological species | Hevea brasiliensis (rubber tree) | ||||||
Method | X-RAY DIFFRACTION / FOURIER SYNTHESIS / Resolution: 2.9 Å | ||||||
Authors | Gruber, K. / Gartler, G. / Krammer, B. / Schwab, H. / Kratky, C. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2004 Title: Reaction mechanism of hydroxynitrile lyases of the alpha/beta-hydrolase superfamily: the three-dimensional structure of the transient enzyme-substrate complex certifies the crucial role of LYS236 Authors: Gruber, K. / Gartler, G. / Krammer, B. / Schwab, H. / Kratky, C. #1: Journal: Biol.Chem. / Year: 1999 Title: Atomic resolution crystal structure of hydroxynitrile lyase from hevea brasiliensis Authors: Gruber, K. / Gugganig, M. / Wagner, U.G. / Kratky, C. #2: Journal: Protein Sci. / Year: 1999 Title: Three-dimensional structures of enzyme-substrate complexes of the hydroxynitrile lyase from hevea brasiliensis Authors: Zuegg, J. / Gruber, K. / Gugganig, M. / Wagner, U.G. / Kratky, C. #3: Journal: Structure / Year: 1996 Title: Mechanism of cyanogenesis: the crystal structure of hydroxynitrile lyase from Hevea brasiliensis Authors: Wagner, U.G. / Hasslacher, M. / Griengl, H. / Schwab, H. / Kratky, C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1scq.cif.gz | 63.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1scq.ent.gz | 47.1 KB | Display | PDB format |
PDBx/mmJSON format | 1scq.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/sc/1scq ftp://data.pdbj.org/pub/pdb/validation_reports/sc/1scq | HTTPS FTP |
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-Related structure data
Related structure data | 1sc9C 1sciC 1sckC 2yasS S: Starting model for refinement C: citing same article (ref.) |
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Similar 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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Details | dimer; the second part of the biological assembly is generated by the two fod axis: x, -y+1, -z. |
-Components
#1: Protein | ( Mass: 29246.578 Da / Num. of mol.: 1 / Mutation: K236L Source method: isolated from a genetically manipulated source Source: (gene. exp.) Hevea brasiliensis (rubber tree) / Tissue: leaf / Gene: HNL / Plasmid: BHIL-D2 / Production host: Pichia pastoris (fungus) / References: UniProt: P52704, EC: 4.1.2.39 | ||
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#2: Chemical | ChemComp-SO4 / #3: Chemical | ChemComp-CNH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.8 Å3/Da / Density % sol: 55.77 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: ammonium sulfate, PEG 400, HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ROTATING ANODE / Type: SIEMENS / Wavelength: 1.5418 Å |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Mar 11, 2001 |
Radiation | Monochromator: graphite / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→10 Å / Num. all: 8029 / Num. obs: 8029 / % possible obs: 87.7 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 2.7 % / Biso Wilson estimate: 25 Å2 / Rsym value: 0.183 / Net I/σ(I): 7.7 |
Reflection shell | Resolution: 2.7→2.79 Å / Mean I/σ(I) obs: 1.9 / Num. unique all: 820 / Rsym value: 0.668 / % possible all: 89.8 |
-Processing
Software |
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Refinement | Method to determine structure: FOURIER SYNTHESIS Starting model: 2yas Resolution: 2.9→9.98 Å / Rfactor Rfree error: 0.017 / Data cutoff high absF: 1297682.85 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber Details: refinement against maximum likelihood target function
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 32.9121 Å2 / ksol: 0.463689 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 24 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.9→9.98 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.9→3 Å / Rfactor Rfree error: 0.07 / Total num. of bins used: 10
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Xplor file |
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