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- PDB-1uel: Solution structure of ubiquitin-like domain of hHR23B complexed w... -
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Basic information
Entry | Database: PDB / ID: 1uel | ||||||
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Title | Solution structure of ubiquitin-like domain of hHR23B complexed with ubiquitin-interacting motif of proteasome subunit S5a | ||||||
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![]() | GENE REGULATION/protein binding / UBL / UIM / RIKEN Structural Genomics/Proteomics Initiative / RSGI / Structural Genomics / GENE REGULATION-protein binding COMPLEX | ||||||
Function / homology | ![]() XPC complex / DNA damage sensor activity / regulation of proteasomal ubiquitin-dependent protein catabolic process / proteasome accessory complex / cellular response to interleukin-7 / proteasome regulatory particle, base subcomplex / Proteasome assembly / proteasome binding / polyubiquitin modification-dependent protein binding / proteasome complex ...XPC complex / DNA damage sensor activity / regulation of proteasomal ubiquitin-dependent protein catabolic process / proteasome accessory complex / cellular response to interleukin-7 / proteasome regulatory particle, base subcomplex / Proteasome assembly / proteasome binding / polyubiquitin modification-dependent protein binding / proteasome complex / Josephin domain DUBs / ubiquitin binding / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / nucleotide-excision repair / DNA Damage Recognition in GG-NER / Formation of Incision Complex in GG-NER / single-stranded DNA binding / spermatogenesis / molecular adaptor activity / RNA polymerase II-specific DNA-binding transcription factor binding / proteasome-mediated ubiquitin-dependent protein catabolic process / damaged DNA binding / RNA polymerase II cis-regulatory region sequence-specific DNA binding / RNA binding / nucleoplasm / identical protein binding / nucleus / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / simulated annealing procedure in CNS, further refined by AMBER 7 | ||||||
![]() | Fujiwara, K. / Tenno, T. / Jee, J.G. / Sugasawa, K. / Ohki, I. / Kojima, C. / Tochio, H. / Hiroaki, H. / Hanaoka, H. / Shirakawa, M. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
![]() | ![]() Title: Structure of the Ubiquitin-interacting Motif of S5a Bound to the Ubiquitin-like Domain of HR23B Authors: Fujiwara, K. / Tenno, T. / Sugasawa, K. / Jee, J.G. / Ohki, I. / Kojima, C. / Tochio, H. / Hiroaki, H. / Hanaoka, F. / Shirakawa, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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PDBx/mmCIF format | ![]() | 862 KB | Display | ![]() |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Similar structure data | |
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Other databases |
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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: 10750.396 Da / Num. of mol.: 1 / Fragment: ubiquitin-like domain (RESIDUES 1-95) Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Protein/peptide | Mass: 5198.620 Da / Num. of mol.: 1 / Fragment: ubiquitin-interacting motif (RESIDUES 201-248) Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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Sample preparation
Details | Contents: U-15N, U-13C Solvent system: 20mM potassium phosphate buffer (pH 6.8), 5mM KCl, 90% H2O, 10% D2O |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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Processing
NMR software | Name: ![]() |
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Refinement | Method: simulated annealing procedure in CNS, further refined by AMBER 7 Software ordinal: 1 Details: RESIDUES INCLUDING MET1 THROUGH THR75 OF HHR23B AND LEU278 THROUGH GLN 296 OF S5A ARE ORDERED IN SOLUTION, WHILE THE REST IS HIGHLY FLEXIBLE (BASED ON 1H-15N HETERONUCLEAR NOE ANALYSIS). |
NMR ensemble | Conformer selection criteria: The submitted conformer models are the 20 structures with the lowest Conformers calculated total number: 100 / Conformers submitted total number: 20 |