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Yorodumi- PDB-7w45: Complex structure of a leaf-branch compost cutinase variant LCC I... -
+Open data
-Basic information
Entry | Database: PDB / ID: 7w45 | ||||||
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Title | Complex structure of a leaf-branch compost cutinase variant LCC ICCG_KIP | ||||||
Components | Leaf-branch compost cutinase | ||||||
Keywords | HYDROLASE / plastic degradation / mutant / catalysis | ||||||
Function / homology | Alpha/beta hydrolase fold-5 / Alpha/beta hydrolase family / poly(ethylene terephthalate) hydrolase / acetylesterase activity / cutinase activity / cutinase / Alpha/Beta hydrolase fold / extracellular region / Leaf-branch compost cutinase Function and homology information | ||||||
Biological species | unidentified prokaryotic organism (environmental samples) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.94 Å | ||||||
Authors | Niu, D. / Zeng, W. / Huang, J.W. / Chen, C.C. / Liu, W.D. / Guo, R.T. | ||||||
Funding support | 1items
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Citation | Journal: Acs Catalysis / Year: 2022 Title: Substrate-Binding Mode of a Thermophilic PET Hydrolase and Engineering the Enzyme to Enhance the Hydrolytic Efficacy. Authors: Zeng, W. / Li, X. / Yang, Y. / Min, J. / Huang, J.-W. / Liu, W. / Niu, D. / Yang, X. / Han, X. / Zhang, L. / Dai, L. / Chen, C.-C. / Guo, R.-T. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7w45.cif.gz | 124.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7w45.ent.gz | 93.3 KB | Display | PDB format |
PDBx/mmJSON format | 7w45.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/w4/7w45 ftp://data.pdbj.org/pub/pdb/validation_reports/w4/7w45 | HTTPS FTP |
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-Related structure data
Related structure data | 7vvcC 7vveC 7w1nC 7w44C 7ds7S 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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-Components
#1: Protein | Mass: 28548.010 Da / Num. of mol.: 2 / Mutation: A59K,V63I,N248P Source method: isolated from a genetically manipulated source Source: (gene. exp.) unidentified prokaryotic organism (environmental samples) Details (production host): pET32a / Production host: Escherichia coli BL21(DE3) (bacteria) References: UniProt: G9BY57, cutinase, poly(ethylene terephthalate) hydrolase #2: Chemical | ChemComp-NA / | #3: Chemical | ChemComp-CA / #4: Water | ChemComp-HOH / | Has ligand of interest | N | |
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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: 2.21 Å3/Da / Density % sol: 44.35 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 6.5 Details: 18 % PEG 8000, 0.2 M Calcium acetate hydrate, 0.1 M Sodium cacodylate trihydate |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N | ||||||||||||||||||||||||||||||
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Diffraction source | Source: LIQUID ANODE / Type: BRUKER METALJET / Wavelength: 1.34138 Å | ||||||||||||||||||||||||||||||
Detector | Type: Bruker PHOTON III / Detector: PIXEL / Date: Sep 26, 2021 | ||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 1.34138 Å / Relative weight: 1 | ||||||||||||||||||||||||||||||
Reflection | Resolution: 1.93→35.44 Å / Num. obs: 37746 / % possible obs: 97.9 % / Redundancy: 5.7 % / CC1/2: 0.994 / Rmerge(I) obs: 0.113 / Rpim(I) all: 0.05 / Rrim(I) all: 0.124 / Net I/σ(I): 10.5 | ||||||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 7DS7 Resolution: 1.94→35.44 Å / Cor.coef. Fo:Fc: 0.959 / Cor.coef. Fo:Fc free: 0.932 / SU B: 3.499 / SU ML: 0.099 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.153 / ESU R Free: 0.141 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 71.56 Å2 / Biso mean: 13.86 Å2 / Biso min: 1.8 Å2
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Refinement step | Cycle: final / Resolution: 1.94→35.44 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.94→1.99 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
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