+Open data
-Basic information
Entry | Database: PDB / ID: 2ckh | |||||||||
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Title | SENP1-SUMO2 complex | |||||||||
Components |
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Keywords | HYDROLASE / UBL CONJUGATION PATHWAY / NUCLEAR PROTEIN / PROTEASE CO- COMPLEX / SUMO / PROTEASE / THIOL PROTEASE | |||||||||
Function / homology | Function and homology information SUMO-specific endopeptidase activity / deSUMOylase activity / SUMO is proteolytically processed / SUMO is conjugated to E1 (UBA2:SAE1) / protein desumoylation / SUMO is transferred from E1 to E2 (UBE2I, UBC9) / Vitamin D (calciferol) metabolism / SUMOylation of SUMOylation proteins / RHOF GTPase cycle / SUMOylation of RNA binding proteins ...SUMO-specific endopeptidase activity / deSUMOylase activity / SUMO is proteolytically processed / SUMO is conjugated to E1 (UBA2:SAE1) / protein desumoylation / SUMO is transferred from E1 to E2 (UBE2I, UBC9) / Vitamin D (calciferol) metabolism / SUMOylation of SUMOylation proteins / RHOF GTPase cycle / SUMOylation of RNA binding proteins / SUMO transferase activity / ubiquitin-like protein ligase binding / SUMOylation of DNA replication proteins / protein sumoylation / SUMOylation of transcription factors / SUMOylation of DNA damage response and repair proteins / regulation of mRNA stability / SUMOylation of chromatin organization proteins / SUMOylation of transcription cofactors / apoptotic signaling pathway / SUMOylation of intracellular receptors / PML body / protein tag activity / Formation of Incision Complex in GG-NER / activation of cysteine-type endopeptidase activity involved in apoptotic process / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / Processing of DNA double-strand break ends / nuclear membrane / endopeptidase activity / Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases / focal adhesion / ubiquitin protein ligase binding / positive regulation of transcription by RNA polymerase II / proteolysis / RNA binding / nucleoplasm / nucleus / cytoplasm Similarity search - Function | |||||||||
Biological species | HOMO SAPIENS (human) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.2 Å | |||||||||
Authors | Shen, L.N. / Dong, C. / Liu, H. / Hay, R.T. / Naismith, J.H. | |||||||||
Citation | Journal: Biochem.J. / Year: 2006 Title: The Structure of Senp1-Sumo-2 Complex Suggests a Structural Basis for Discrimination between Sumo Paralogues During Processing. Authors: Shen, L.N. / Dong, C. / Liu, H. / Naismith, J.H. / Hay, R.T. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2ckh.cif.gz | 74.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2ckh.ent.gz | 55.6 KB | Display | PDB format |
PDBx/mmJSON format | 2ckh.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ck/2ckh ftp://data.pdbj.org/pub/pdb/validation_reports/ck/2ckh | HTTPS FTP |
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-Related structure data
Related structure data | 2ckgC 1tgzS C: citing same article (ref.) 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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Unit cell |
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-Components
#1: Protein | Mass: 26803.098 Da / Num. of mol.: 1 / Fragment: PROTEASE DOMAIN, RESIDUES 419-643 Source method: isolated from a genetically manipulated source Details: COVALENTLY LINKED TO SUMO / Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) References: UniProt: Q9P0U3, Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases |
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#2: Protein | Mass: 9063.168 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P61956 |
Compound details | DEGRADES UBL1 AND SMT3H2 CONJUGATES |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 6.06 Å3/Da / Density % sol: 79.54 % |
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Crystal grow | pH: 5 / Details: pH 5.00 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-1 / Wavelength: 0.933 |
Detector | Type: ADSC QUANTUM 210 / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.933 Å / Relative weight: 1 |
Reflection | Resolution: 3.2→120 Å / Num. obs: 13469 / % possible obs: 100 % / Observed criterion σ(I): 0 / Redundancy: 8.3 % / Rmerge(I) obs: 0.088 / Net I/σ(I): 19.6 |
Reflection shell | Resolution: 3.2→3.3 Å / Redundancy: 8.5 % / Rmerge(I) obs: 0.436 / Mean I/σ(I) obs: 3.3 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1TGZ Resolution: 3.2→124.03 Å / Cor.coef. Fo:Fc: 0.937 / Cor.coef. Fo:Fc free: 0.912 / SU B: 62.802 / SU ML: 0.439 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.689 / ESU R Free: 0.415 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. ANY DISCREPANCY BETWEEN R-FACTORS CALCULATED BY SFCHECK AND/OR EDS MAY BE DUE TO THE USE OF TLS IN THE REFIMNEMENT OF THE STRUCTURE AS INDICATED ABOVE.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 129.72 Å2
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Refinement step | Cycle: LAST / Resolution: 3.2→124.03 Å
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Refine LS restraints |
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