+Open data
-Basic information
Entry | Database: PDB / ID: 6lix | ||||||
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Title | CRL Protein of Arabidopsis | ||||||
Components | Chromophore lyase CRL, chloroplastic | ||||||
Keywords | LYASE / a homolog of cyanobacterial CpcT lyase / PLANT PROTEIN | ||||||
Function / homology | Function and homology information transport of virus in host, tissue to tissue / plastid fission / protein-phycocyanobilin linkage / chloroplast outer membrane / Lyases / chloroplast fission / plastid / regulation of cell division / response to reactive oxygen species / cellular response to virus ...transport of virus in host, tissue to tissue / plastid fission / protein-phycocyanobilin linkage / chloroplast outer membrane / Lyases / chloroplast fission / plastid / regulation of cell division / response to reactive oxygen species / cellular response to virus / defense response / lyase activity / cell cycle / cell division Similarity search - Function | ||||||
Biological species | Arabidopsis thaliana (thale cress) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.385 Å | ||||||
Authors | Wang, F.F. / Guan, K.L. / Sun, P.K. / Xing, W.M. | ||||||
Funding support | China, 1items
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Citation | Journal: Plant J. / Year: 2020 Title: The Arabidopsis CRUMPLED LEAF protein, a homolog of the cyanobacterial bilin lyase, retains the bilin-binding pocket for a yet unknown function. Authors: Wang, F. / Fang, J. / Guan, K. / Luo, S. / Dogra, V. / Li, B. / Ma, D. / Zhao, X. / Lee, K.P. / Sun, P. / Xin, J. / Liu, T. / Xing, W. / Kim, C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6lix.cif.gz | 90.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6lix.ent.gz | 71.2 KB | Display | PDB format |
PDBx/mmJSON format | 6lix.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/li/6lix ftp://data.pdbj.org/pub/pdb/validation_reports/li/6lix | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 30369.145 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: CRL, CAA33, At5g51020, K3K7.20 / Production host: Escherichia coli K-12 (bacteria) / Strain (production host): K-12 / References: UniProt: Q9FI46, Lyases #2: Chemical | #3: 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 grow | Temperature: 277 K / Method: vapor diffusion / Details: 0.1 M MES pH 6.5, 12% PEG 20000 |
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-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL18U1 / Wavelength: 0.9779 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Mar 12, 2016 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 0.9779 Å / Relative weight: 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 2.38→50 Å / Num. obs: 14787 / % possible obs: 99.5 % / Redundancy: 6.8 % / Rmerge(I) obs: 0.077 / Rpim(I) all: 0.032 / Rrim(I) all: 0.083 / Χ2: 0.958 / Net I/σ(I): 6.5 / Num. measured all: 100253 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1
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-Processing
Software |
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Refinement | Method to determine structure: SAD / Resolution: 2.385→49.476 Å / SU ML: 0.29 / Cross valid method: THROUGHOUT / σ(F): 1.38 / Phase error: 28.82
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 92.51 Å2 / Biso mean: 47.7188 Å2 / Biso min: 20.47 Å2 | ||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 2.385→49.476 Å
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0
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