+Open data
-Basic information
Entry | Database: PDB / ID: 5d2m | ||||||
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Title | Complex between human SUMO2-RANGAP1, UBC9 and ZNF451 | ||||||
Components |
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Keywords | Ligase / Protein Binding / Complex / SUMO / E3 Ligase | ||||||
Function / homology | Function and homology information : / cellular response to vasopressin / negative regulation of transcription initiation by RNA polymerase II / positive regulation of SUMO transferase activity / SUMO conjugating enzyme activity / cytoplasmic periphery of the nuclear pore complex / RING-like zinc finger domain binding / SUMO ligase activity / SUMO ligase complex / SUMOylation of nuclear envelope proteins ...: / cellular response to vasopressin / negative regulation of transcription initiation by RNA polymerase II / positive regulation of SUMO transferase activity / SUMO conjugating enzyme activity / cytoplasmic periphery of the nuclear pore complex / RING-like zinc finger domain binding / SUMO ligase activity / SUMO ligase complex / SUMOylation of nuclear envelope proteins / transferase complex / Negative regulation of activity of TFAP2 (AP-2) family transcription factors / SUMO is proteolytically processed / SUMO is conjugated to E1 (UBA2:SAE1) / SUMO is transferred from E1 to E2 (UBE2I, UBC9) / mitotic nuclear membrane reassembly / nuclear pore cytoplasmic filaments / Vitamin D (calciferol) metabolism / synaptonemal complex / small protein activating enzyme binding / SUMOylation of DNA methylation proteins / SUMOylation of immune response proteins / SUMOylation of SUMOylation proteins / Maturation of nucleoprotein / Transferases; Acyltransferases; Aminoacyltransferases / activation of GTPase activity / negative regulation of protein export from nucleus / Rev-mediated nuclear export of HIV RNA / SUMOylation of RNA binding proteins / nuclear export / aggresome / SUMO transferase activity / Postmitotic nuclear pore complex (NPC) reformation / Maturation of nucleoprotein / nucleocytoplasmic transport / SUMOylation of ubiquitinylation proteins / ubiquitin-like protein ligase binding / SUMOylation of DNA replication proteins / protein sumoylation / transcription factor binding / SUMOylation of transcription factors / response to axon injury / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / SUMOylation of DNA damage response and repair proteins / nuclear pore / Mitotic Prometaphase / SARS-CoV-1 targets host intracellular signalling and regulatory pathways / EML4 and NUDC in mitotic spindle formation / axon cytoplasm / Resolution of Sister Chromatid Cohesion / Meiotic synapsis / GTPase activator activity / SUMOylation of chromatin organization proteins / SUMOylation of transcription cofactors / chromosome segregation / RHO GTPases Activate Formins / transcription coregulator binding / negative regulation of transforming growth factor beta receptor signaling pathway / protein modification process / SUMOylation of intracellular receptors / PKR-mediated signaling / PML body / mitotic spindle / kinetochore / protein tag activity / small GTPase binding / Formation of Incision Complex in GG-NER / Separation of Sister Chromatids / transcription corepressor activity / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / nuclear envelope / Processing of DNA double-strand break ends / ubiquitin-dependent protein catabolic process / regulation of gene expression / nuclear membrane / positive regulation of cell migration / cadherin binding / cell division / intracellular membrane-bounded organelle / negative regulation of DNA-templated transcription / dendrite / ubiquitin protein ligase binding / perinuclear region of cytoplasm / negative regulation of transcription by RNA polymerase II / enzyme binding / signal transduction / positive regulation of transcription by RNA polymerase II / RNA binding / nucleoplasm / ATP binding / metal ion binding / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å | ||||||
Authors | Cappadocia, L. / Lima, C.D. | ||||||
Funding support | United States, 1items
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Citation | Journal: Nat.Struct.Mol.Biol. / Year: 2015 Title: Structural basis for catalytic activation by the human ZNF451 SUMO E3 ligase. Authors: Cappadocia, L. / Pichler, A. / Lima, C.D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5d2m.cif.gz | 481.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5d2m.ent.gz | 402.4 KB | Display | PDB format |
PDBx/mmJSON format | 5d2m.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/d2/5d2m ftp://data.pdbj.org/pub/pdb/validation_reports/d2/5d2m | HTTPS FTP |
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-Related structure data
Related structure data | 3uioS S: Starting model for refinement |
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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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Details | Authors state that although a heptameric complex that encompasses all chains present in the asymmetric unit was detected by size exclusion chromatography, structural and biochemical analyses suggest that the biological unit consists of a RANGAP1-SUMO2/UBC9/SUMO2/ZNF451 complex composed of chains A, B, C, E and G. |
-Components
-Protein , 4 types, 7 molecules ADBECFG
#1: Protein | Mass: 18341.107 Da / Num. of mol.: 2 / Mutation: K14R Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: UBE2I, UBC9, UBCE9 / Plasmid: pET28B / Production host: Escherichia coli BL21(DE3) (bacteria) References: UniProt: P63279, Ligases; Forming carbon-nitrogen bonds; Acid-amino-acid ligases (peptide synthases) #2: Protein | Mass: 9476.639 Da / Num. of mol.: 2 / Fragment: UNP residues 15-93 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SUMO2, SMT3B, SMT3H2 / Plasmid: pET28b / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P61956 #3: Protein | Mass: 18573.451 Da / Num. of mol.: 2 / Fragment: UNP residues 418-587 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: RANGAP1, KIAA1835, SD / Plasmid: pSmt3 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P46060 #4: Protein | | Mass: 6907.192 Da / Num. of mol.: 1 / Fragment: UNP residues 2-56 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ZNF451, COASTER, KIAA0576, KIAA1702 / Plasmid: pLou3 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q9Y4E5 |
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-Non-polymers , 2 types, 707 molecules
#5: Chemical | ChemComp-EDO / #6: Water | ChemComp-HOH / | |
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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: 2.96 Å3/Da / Density % sol: 58.45 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 6 % (w/v) PEG 8000, 0.2 M ammonium citrate and 0.1 M HEPES pH 7.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X29A / Wavelength: 1.075 Å |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: May 30, 2014 |
Radiation | Monochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.075 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→46.35 Å / Num. obs: 46766 / % possible obs: 99.6 % / Observed criterion σ(I): -3 / Redundancy: 7.3 % / Biso Wilson estimate: 49 Å2 / Rmerge(I) obs: 0.12 / Net I/σ(I): 10.94 |
Reflection shell | Resolution: 2.4→2.486 Å / Redundancy: 7.3 % / Rmerge(I) obs: 0.5143 / Mean I/σ(I) obs: 3.83 / % possible all: 96.6 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 3UIO Resolution: 2.4→46.349 Å / SU ML: 0.22 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 21.85 / 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 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.4→46.349 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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