+Open data
-Basic information
Entry | Database: PDB / ID: 6ww3 | ||||||
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Title | Crystal structure of HERC2 ZZ domain in complex with SUMO1 tail | ||||||
Components | SUMO1 linked HERC2 ZZ domain (Small ubiquitin-related modifier 1,E3 ubiquitin-protein ligase HERC2) | ||||||
Keywords | GENE REGULATION / Zn finger protein / ZZ domain / HERC2 | ||||||
Function / homology | Function and homology information negative regulation of transcription by transcription factor localization / SUMOylation of nuclear envelope proteins / Negative regulation of activity of TFAP2 (AP-2) family transcription factors / SUMO is proteolytically processed / negative regulation of delayed rectifier potassium channel activity / SUMO is conjugated to E1 (UBA2:SAE1) / nuclear stress granule / SUMO is transferred from E1 to E2 (UBE2I, UBC9) / negative regulation of action potential / SUMO binding ...negative regulation of transcription by transcription factor localization / SUMOylation of nuclear envelope proteins / Negative regulation of activity of TFAP2 (AP-2) family transcription factors / SUMO is proteolytically processed / negative regulation of delayed rectifier potassium channel activity / SUMO is conjugated to E1 (UBA2:SAE1) / nuclear stress granule / SUMO is transferred from E1 to E2 (UBE2I, UBC9) / negative regulation of action potential / SUMO binding / small protein activating enzyme binding / SUMOylation of DNA methylation proteins / HECT-type E3 ubiquitin transferase / SUMOylation of immune response proteins / SUMOylation of SUMOylation proteins / Maturation of nucleoprotein / SUMOylation of RNA binding proteins / Postmitotic nuclear pore complex (NPC) reformation / Maturation of nucleoprotein / negative regulation of protein import into nucleus / ubiquitin-specific protease binding / roof of mouth development / SUMOylation of ubiquitinylation proteins / negative regulation of DNA binding / ubiquitin-like protein ligase binding / SUMOylation of DNA replication proteins / protein sumoylation / transcription factor binding / SUMOylation of transcription factors / potassium channel regulator activity / SUMOylation of DNA damage response and repair proteins / Regulation of IFNG signaling / nuclear pore / cellular response to cadmium ion / centriole / SUMOylation of chromatin organization proteins / guanyl-nucleotide exchange factor activity / SUMOylation of transcription cofactors / positive regulation of protein-containing complex assembly / Nonhomologous End-Joining (NHEJ) / intracellular protein transport / SUMOylation of intracellular receptors / PKR-mediated signaling / G2/M DNA damage checkpoint / negative regulation of DNA-binding transcription factor activity / PML body / protein tag activity / Formation of Incision Complex in GG-NER / regulation of protein localization / ubiquitin protein ligase activity / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / Antigen processing: Ubiquitination & Proteasome degradation / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / cellular response to heat / Processing of DNA double-strand break ends / spermatogenesis / proteasome-mediated ubiquitin-dependent protein catabolic process / nuclear membrane / protein stabilization / protein ubiquitination / nuclear body / nuclear speck / DNA repair / negative regulation of DNA-templated transcription / DNA damage response / ubiquitin protein ligase binding / nucleolus / enzyme binding / RNA binding / zinc ion binding / nucleoplasm / membrane / nucleus / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.096 Å | ||||||
Authors | Liu, J. / Vann, K.R. / Kutateladze, T.G. | ||||||
Citation | Journal: Structure / Year: 2020 Title: Structural Insight into Binding of the ZZ Domain of HERC2 to Histone H3 and SUMO1. Authors: Liu, J. / Xue, Z. / Zhang, Y. / Vann, K.R. / Shi, X. / Kutateladze, T.G. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6ww3.cif.gz | 42.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6ww3.ent.gz | 27.3 KB | Display | PDB format |
PDBx/mmJSON format | 6ww3.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ww/6ww3 ftp://data.pdbj.org/pub/pdb/validation_reports/ww/6ww3 | HTTPS FTP |
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-Related structure data
Related structure data | 6ww4C 6ds6S 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: 6909.763 Da / Num. of mol.: 2 / Fragment: fusion protein Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SUMO1, SMT3C, SMT3H3, UBL1, OK/SW-cl.43, HERC2 / Production host: Escherichia coli (E. coli) References: UniProt: P63165, UniProt: O95714, HECT-type E3 ubiquitin transferase #2: Chemical | ChemComp-ZN / #3: Chemical | ChemComp-PEG / | #4: Chemical | ChemComp-GOL / | #5: Water | ChemComp-HOH / | Has ligand of interest | N | Sequence details | Residues 2-7 of SUMO1 fused to the ZZ domain of HERC2 | |
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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: 1.99 Å3/Da / Density % sol: 38.08 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop Details: 0.2 M ammonium chloride, 0.1 M Tris, pH 8.0 and 20% PEG 6000 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU MICROMAX-007 HF / Wavelength: 1.54 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: DECTRIS PILATUS 200K / Detector: PIXEL / Date: Oct 22, 2018 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 1.95→50 Å / Num. obs: 7588 / % possible obs: 89.2 % / Redundancy: 3 % / Biso Wilson estimate: 13.18 Å2 / Rmerge(I) obs: 0.181 / Rpim(I) all: 0.113 / Rrim(I) all: 0.215 / Χ2: 1.062 / Net I/σ(I): 3.5 / Num. measured all: 22967 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 6DS6 Resolution: 2.096→33.426 Å / SU ML: 0.19 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 21.17 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||
Displacement parameters | Biso max: 42.5 Å2 / Biso mean: 14.5705 Å2 / Biso min: 4.74 Å2 | ||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 2.096→33.426 Å
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Refine LS restraints |
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0
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