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- PDB-4izv: The E41Q/C145A double mutant of the amidase from Nesterenkonia sp... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4izv | ||||||
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Title | The E41Q/C145A double mutant of the amidase from Nesterenkonia sp. AN1 in complex with acrylamide | ||||||
![]() | Amidase | ||||||
![]() | hydrolase/substrate / hydrolase / active site / acrylamide (prop-2-enamide) / cysteine 145 / hydrolase-substrate complex | ||||||
Function / homology | ![]() indoleacetamide hydrolase activity / amidase / N-carbamoylputrescine amidase activity / putrescine biosynthetic process from arginine / beta-alanine biosynthetic process via 3-ureidopropionate / beta-ureidopropionase activity / amidase activity Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() ![]() | ||||||
![]() | Kimani, S.W. / Sewell, B.T. | ||||||
![]() | ![]() Title: Covalent modifications of the active site cysteine occur as a result of mutating the glutamate of the catalytic triad in the amidase from Nesterenkonia sp. Authors: Kimani, S.W. / Hunter, R. / Vlok, M. / Watermeyer, J. / Sewell, B.T. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 65.9 KB | Display | ![]() |
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PDB format | ![]() | 51.4 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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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 30067.701 Da / Num. of mol.: 1 / Mutation: E41Q, C145A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||
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#2: Chemical | ChemComp-ROP / | ||
#3: Chemical | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.36 Å3/Da / Density % sol: 47.95 % |
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Crystal grow | Temperature: 298 K Details: 2.0 M ammonium sulfate, vapor diffusion, sitting drop, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Detector: CCD / Date: Nov 14, 2010 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.8856 Å / Relative weight: 1 |
Reflection | Resolution: 1.65→43.213 Å / Num. obs: 34247 / % possible obs: 98.9 % / Redundancy: 6.9 % / Rsym value: 0.074 / Net I/σ(I): 18 |
Reflection shell | Resolution: 1.65→1.74 Å / Redundancy: 6.1 % / Rmerge(I) obs: 0.389 / Mean I/σ(I) obs: 1.7 / Rsym value: 0.389 / % possible all: 93.4 |
-Phasing
Phasing | Method: ![]() | |||||||||
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Phasing MR | Rfactor: 29.08 / Model details: Phaser MODE: MR_AUTO
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 18.13 Å2
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Refinement step | Cycle: LAST / Resolution: 1.65→37.72 Å
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Refine LS restraints |
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