+Open data
-Basic information
Entry | Database: PDB / ID: 2io0 | ||||||
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Title | Crystal structure of human Senp2 in complex with preSUMO-2 | ||||||
Components |
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Keywords | PROTEIN BINDING / HYDROLASE / SUMO / Ubiquitin / Senp / Ulp / complex | ||||||
Function / homology | Function and homology information SUMO-specific endopeptidase activity / SUMO is proteolytically processed / SUMO is conjugated to E1 (UBA2:SAE1) / deSUMOylase activity / protein desumoylation / SUMO is transferred from E1 to E2 (UBE2I, UBC9) / Vitamin D (calciferol) metabolism / SUMOylation of SUMOylation proteins / regulation of Wnt signaling pathway / SUMOylation of RNA binding proteins ...SUMO-specific endopeptidase activity / SUMO is proteolytically processed / SUMO is conjugated to E1 (UBA2:SAE1) / deSUMOylase activity / protein desumoylation / SUMO is transferred from E1 to E2 (UBE2I, UBC9) / Vitamin D (calciferol) metabolism / SUMOylation of SUMOylation proteins / regulation of Wnt signaling pathway / SUMOylation of RNA binding proteins / SUMO transferase activity / fat cell differentiation / ubiquitin-like protein ligase binding / SUMOylation of DNA replication proteins / protein sumoylation / SUMOylation of transcription factors / mRNA transport / SUMOylation of DNA damage response and repair proteins / nuclear pore / negative regulation of protein ubiquitination / SUMOylation of chromatin organization proteins / SUMOylation of transcription cofactors / positive regulation of protein ubiquitination / protein destabilization / SUMOylation of intracellular receptors / PML body / Wnt signaling pathway / Formation of Incision Complex in GG-NER / protein tag activity / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / protein transport / Processing of DNA double-strand break ends / nuclear membrane / Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases / ubiquitin protein ligase binding / positive regulation of transcription by RNA polymerase II / proteolysis / RNA binding / nucleoplasm / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.3 Å | ||||||
Authors | Reverter, D. / Lima, C.D. | ||||||
Citation | Journal: Nat.Struct.Mol.Biol. / Year: 2006 Title: Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates. Authors: Reverter, D. / 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 | 2io0.cif.gz | 81.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2io0.ent.gz | 60.5 KB | Display | PDB format |
PDBx/mmJSON format | 2io0.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/io/2io0 ftp://data.pdbj.org/pub/pdb/validation_reports/io/2io0 | HTTPS FTP |
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-Related structure data
Related structure data | 2io1C 2io2C 2io3C 1tgzS 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: 27342.648 Da / Num. of mol.: 1 / Fragment: catalytic domain / Mutation: C548S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SENP2, KIAA1331 / Plasmid: pET28b / Production host: Escherichia coli (E. coli) References: UniProt: Q9HC62, Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases | ||
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#2: Protein | Mass: 10598.898 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SUMO2, SMT3B, SMT3H2 / Plasmid: pET28b / Production host: Escherichia coli (E. coli) / References: UniProt: P61956 | ||
#3: Chemical | #4: 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: 2.83 Å3/Da / Density % sol: 56.57 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 8 Details: 15% PEG 4000, 0.2M Lithium sulfate, 0.1mM Tris-HCl, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 0.9795 Å |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Aug 10, 2005 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9795 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→50 Å / Num. all: 18192 / Num. obs: 18192 / % possible obs: 94.8 % / Observed criterion σ(I): 0 / Redundancy: 7.3 % / Rmerge(I) obs: 0.042 / Χ2: 0.715 / Net I/σ(I): 16.5 |
Reflection shell | Resolution: 2.3→2.38 Å / Redundancy: 3.9 % / Rmerge(I) obs: 0.256 / Mean I/σ(I) obs: 2.3 / Num. unique all: 1651 / Χ2: 0.299 / % possible all: 86.7 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1TGZ Resolution: 2.3→48.3 Å / Rfactor Rfree error: 0.008 / FOM work R set: 0.82 / Data cutoff high absF: 3134411.75 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 58.425 Å2 / ksol: 0.353 e/Å3 | ||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 52.5 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.3→48.3 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.3→2.44 Å / Rfactor Rfree error: 0.03 / Total num. of bins used: 6
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Xplor file |
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