+Open data
-Basic information
Entry | Database: PDB / ID: 7ep3 | ||||||||||||
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Title | Crystal structure of ZER1 bound to GAGN degron | ||||||||||||
Components | Protein zer-1 homolog | ||||||||||||
Keywords | LIGASE / E3 ligase | ||||||||||||
Function / homology | Cul2-RING ubiquitin ligase complex / protein quality control for misfolded or incompletely synthesized proteins / Armadillo/beta-catenin-like repeats / Armadillo / Leucine-rich repeat domain superfamily / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / Armadillo-like helical / Armadillo-type fold / Protein zer-1 homolog Function and homology information | ||||||||||||
Biological species | Homo sapiens (human) | ||||||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.513 Å | ||||||||||||
Authors | Yan, X. / Li, Y. | ||||||||||||
Funding support | China, 3items
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Citation | Journal: Mol.Cell / Year: 2021 Title: Molecular basis for recognition of Gly/N-degrons by CRL2 ZYG11B and CRL2 ZER1 . Authors: Yan, X. / Li, Y. / Wang, G. / Zhou, Z. / Song, G. / Feng, Q. / Zhao, Y. / Mi, W. / Ma, Z. / Dong, C. | ||||||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7ep3.cif.gz | 65.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7ep3.ent.gz | 45.2 KB | Display | PDB format |
PDBx/mmJSON format | 7ep3.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ep/7ep3 ftp://data.pdbj.org/pub/pdb/validation_reports/ep/7ep3 | HTTPS FTP |
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-Related structure data
Related structure data | 7ep0SC 7ep1C 7ep2C 7ep4C 7ep5C 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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Unit cell |
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-Components
#1: Protein | Mass: 28982.477 Da / Num. of mol.: 1 / Fragment: UNP residues 520-766 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ZER1, C9orf60, ZYG, ZYG11BL / Production host: Escherichia coli (E. coli) / References: UniProt: Q7Z7L7 |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.48 Å3/Da / Density % sol: 50.34 % Description: THE ENTRY CONTAINS FRIEDEL PAIRS IN I_PLUS/MINUS COLUMNS. |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, sitting drop Details: 0.2 M Sodium formate, 23% (wt/vol) Polyethylene glycol 3,350, 0.033% (wt/vol) Anthrone, 0.033% (wt/vol) Congo Red, 0.033% (wt/vol) N-(2-Acetamido)-2-aminoethanesulfonic acid, 0.002 M HEPES sodium pH 6.8 |
-Data collection
Diffraction | Mean temperature: 80 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL17U1 / Wavelength: 0.979191 Å |
Detector | Type: MAR CCD 165 mm / Detector: CCD / Date: Dec 26, 2020 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.979191 Å / Relative weight: 1 |
Reflection | Resolution: 1.51→59.19 Å / Num. obs: 43366 / % possible obs: 98.8 % / Redundancy: 11 % / Biso Wilson estimate: 23.2 Å2 / Rmerge(I) obs: 0.038 / Net I/σ(I): 30.6 |
Reflection shell | Resolution: 1.51→1.55 Å / Rmerge(I) obs: 0.44 / Mean I/σ(I) obs: 2.8 / Num. unique obs: 2864 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 7EP0 Resolution: 1.513→22.323 Å / Cross valid method: FREE R-VALUE Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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Displacement parameters | Biso mean: 28.5 Å2 | ||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.513→22.323 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.513→1.567 Å
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