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- PDB-1f4i: SOLUTION STRUCTURE OF THE HHR23A UBA(2) MUTANT P333E, DEFICIENT I... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1f4i | ||||||
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Title | SOLUTION STRUCTURE OF THE HHR23A UBA(2) MUTANT P333E, DEFICIENT IN BINDING THE HIV-1 ACCESSORY PROTEIN VPR | ||||||
![]() | UV EXCISION REPAIR PROTEIN PROTEIN RAD23 HOMOLOG A | ||||||
![]() | DNA BINDING PROTEIN / TRANSCRIPTION / alpha helical bundle | ||||||
Function / homology | ![]() regulation of proteasomal ubiquitin-dependent protein catabolic process / proteasome binding / ubiquitin-specific protease binding / polyubiquitin modification-dependent protein binding / positive regulation of viral genome replication / positive regulation of cell cycle / proteasome complex / Josephin domain DUBs / ubiquitin binding / nucleotide-excision repair ...regulation of proteasomal ubiquitin-dependent protein catabolic process / proteasome binding / ubiquitin-specific protease binding / polyubiquitin modification-dependent protein binding / positive regulation of viral genome replication / positive regulation of cell cycle / proteasome complex / Josephin domain DUBs / ubiquitin binding / nucleotide-excision repair / DNA Damage Recognition in GG-NER / protein destabilization / kinase binding / Formation of Incision Complex in GG-NER / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / single-stranded DNA binding / proteasome-mediated ubiquitin-dependent protein catabolic process / damaged DNA binding / intracellular membrane-bounded organelle / Golgi apparatus / protein-containing complex / nucleoplasm / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Method | SOLUTION NMR / simulated annealing, distance geometry | ||||||
![]() | Withers-Ward, E.S. / Mueller, T.D. / Chen, I.S. / Feigon, J. | ||||||
![]() | ![]() Title: Biochemical and structural analysis of the interaction between the UBA(2) domain of the DNA repair protein HHR23A and HIV-1 Vpr. Authors: Withers-Ward, E.S. / Mueller, T.D. / Chen, I.S. / Feigon, J. #1: ![]() Title: Structure of a human DNA repair protein UBA domain that interacts with HIV-1 Vpr Authors: Dieckmann, T. / Withers-Ward, E.S. / Jarosinski, M.A. / Liu, C.F. / Chen, I.S.Y. / Feigon, J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 293.8 KB | Display | ![]() |
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PDB format | ![]() | 244.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 346.2 KB | Display | ![]() |
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Full document | ![]() | 485.3 KB | Display | |
Data in XML | ![]() | 17.6 KB | Display | |
Data in CIF | ![]() | 29.4 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/peptide | Mass: 5183.710 Da / Num. of mol.: 1 / Fragment: C-TERMINAL UBA DOMAIN / Mutation: P333E / Source method: obtained synthetically Details: THIS PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE OF THIS PEPTIDE NATURALLY OCCURS IN HUMANS (HOMO SAPIENS). References: UniProt: P54725 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR experiment | Type: 2D NOESY |
NMR details | Text: This structure was determined using standard 2D homonuclear techniques |
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Sample preparation
Details | Contents: 2mM UBA(2) domain mutant P333E; 50mM phosphate buffer, 150mM sodium chloride; 90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 50mM sodium phosphate, 150mM sodium chloride pH: 6.5 / Pressure: ambient / Temperature: 300 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: simulated annealing, distance geometry / Software ordinal: 1 Details: total number of restraints 826, 204 intraresidual, 182 sequential, 226 medium range (|i-j|<5), 214 long range (|i-j|>=5) | ||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 21 |