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Open data
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Basic information
Entry | Database: PDB / ID: 5ghc | |||||||||
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Title | SOLUTION STRUCTURE OF LYS33 ACETYLATED HUMAN SUMO2 | |||||||||
![]() | Small ubiquitin-related modifier 2 | |||||||||
![]() | STRUCTURAL GENOMICS / UBIQUITIN-LIKE PROTEIN / ACETYLATED PROTEIN | |||||||||
Function / homology | ![]() SUMO is proteolytically processed / SUMO is conjugated to E1 (UBA2:SAE1) / SUMO is transferred from E1 to E2 (UBE2I, UBC9) / Vitamin D (calciferol) metabolism / SUMOylation of SUMOylation proteins / SUMOylation of RNA binding proteins / ubiquitin-like protein ligase binding / SUMOylation of DNA replication proteins / SUMOylation of transcription factors / protein sumoylation ...SUMO is proteolytically processed / SUMO is conjugated to E1 (UBA2:SAE1) / SUMO is transferred from E1 to E2 (UBE2I, UBC9) / Vitamin D (calciferol) metabolism / SUMOylation of SUMOylation proteins / SUMOylation of RNA binding proteins / ubiquitin-like protein ligase binding / SUMOylation of DNA replication proteins / SUMOylation of transcription factors / protein sumoylation / SUMOylation of DNA damage response and repair proteins / SUMOylation of chromatin organization proteins / SUMOylation of transcription cofactors / SUMOylation of intracellular receptors / PML body / Formation of Incision Complex in GG-NER / protein tag activity / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / Processing of DNA double-strand break ends / ubiquitin protein ligase binding / RNA binding / nucleoplasm / nucleus Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | SOLUTION NMR / TORSION ANGLE DYNAMICS, DGSA- DISTANCE GEOMETRY SIMULATED ANNEALING | |||||||||
![]() | Naik, M.T. / Naik, N. / Shih, H. / Huang, T. | |||||||||
![]() | ![]() Title: Structures Of Human Sumo Authors: Naik, M.T. / Naik, N. / Shih, H. / Huang, T. | |||||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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PDBx/mmCIF format | ![]() | 577.6 KB | Display | ![]() |
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PDB format | ![]() | 481.9 KB | Display | ![]() |
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-Validation report
Summary document | ![]() | 413.6 KB | Display | ![]() |
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Full document | ![]() | 555.7 KB | Display | |
Data in XML | ![]() | 30.8 KB | Display | |
Data in CIF | ![]() | 51.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 12283.632 Da / Num. of mol.: 1 / Fragment: UNP RESIDUES 1-93 Source method: isolated from a genetically manipulated source Details: Lys33 acetylated mature SMALL UBIQUITIN-RELATED MODIFIER 2 (SUMO2) Residues 1-14 (MGSSHHHHHHSQDP) represent a non-native purification tag. These residues were neither assigned nor included ...Details: Lys33 acetylated mature SMALL UBIQUITIN-RELATED MODIFIER 2 (SUMO2) Residues 1-14 (MGSSHHHHHHSQDP) represent a non-native purification tag. These residues were neither assigned nor included in structure calculation. Source: (gene. exp.) ![]() Description: PLASMID PCDF PYLT-1 WITH SUMO INSERT WITH K33STOP MUTATION (WITH AMBER CODON) AND PACKRS-3 AS DESCRIBED IN NEUMANN ET AL., MOL CELL, 36, 153, 2009 Gene: SUMO2, SMT3B, SMT3H2 Details (production host): Plasmid pCDF PylT-1 with SUMO insert with K33STOP mutation (with amber codon) and pAcKRS-3 as described in Neumann et al., Mol Cell, 36, 153, 2009 Production host: ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: NMR DATA WAS ACQUIRED AT 295K USING SHIGEMI NMR TUBES. |
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Sample preparation
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