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Open data
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Basic information
Entry | Database: PDB / ID: 1f9c | ||||||
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Title | CRYSTAL STRUCTURE OF MLE D178N VARIANT | ||||||
![]() | PROTEIN (MUCONATE CYCLOISOMERASE I) | ||||||
![]() | ISOMERASE / THERMOSTABLE MUTANT | ||||||
Function / homology | ![]() chloromuconate cycloisomerase activity / muconate cycloisomerase activity / amino acid catabolic process / : / manganese ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Kajander, T. / Lehtio, L. / Kahn, P.C. / Goldman, A. | ||||||
![]() | ![]() Title: Buried charged surface in proteins. Authors: Kajander, T. / Kahn, P.C. / Passila, S.H. / Cohen, D.C. / Lehtio, L. / Adolfsen, W. / Warwicker, J. / Schell, U. / Goldman, A. #1: ![]() Title: The Refined Crystal Structure of Muconate Lactonising Enzyme from Pseudomonas putida PRS2000 at 1.85 Resolution Authors: Helin, S. / Kahn, P.C. / Guha, B.L. / Mallows, D.G. / Goldman, A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 137.5 KB | Display | ![]() |
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PDB format | ![]() | 109.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar 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
#1: Protein | Mass: 40107.832 Da / Num. of mol.: 2 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.42 Å3/Da / Density % sol: 49.28 % |
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Crystal grow | Temperature: 277 K / Method: microdialysis / pH: 6.5 Details: MES, NaCl, MnCl2, beta-mercaptoethanol, NaN3, pH 6.5, MICRODIALYSIS, temperature 277K |
-Data collection
Diffraction | Mean temperature: 103 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Sep 1, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.92 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→20 Å / Num. obs: 22444 / % possible obs: 87 % / Rmerge(I) obs: 0.046 |
Reflection | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 20 Å |
Reflection shell | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 2.6 Å / % possible obs: 59.3 % |
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Processing
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Refinement | Resolution: 2.5→8 Å / σ(F): 2
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Refinement step | Cycle: LAST / Resolution: 2.5→8 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS % reflection Rfree: 5 % / Rfactor all: 0.187 / Rfactor obs: 0.18 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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