+Open data
-Basic information
Entry | Database: PDB / ID: 1tp4 | ||||||
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Title | Solution structure of the XPC binding domain of hHR23A protein | ||||||
Components | UV excision repair protein RAD23 homolog A | ||||||
Keywords | DNA REPAIR / NER / XPC / Rad23 | ||||||
Function / homology | Function and homology information 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 | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / distance geometry | ||||||
Authors | Kamionka, M. / Feigon, J. | ||||||
Citation | Journal: Protein Sci. / Year: 2004 Title: Structure of the XPC binding domain of hHR23A reveals hydrophobic patches for protein interaction Authors: Kamionka, M. / Feigon, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1tp4.cif.gz | 478.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1tp4.ent.gz | 394.4 KB | Display | PDB format |
PDBx/mmJSON format | 1tp4.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1tp4_validation.pdf.gz | 343.6 KB | Display | wwPDB validaton report |
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Full document | 1tp4_full_validation.pdf.gz | 579.9 KB | Display | |
Data in XML | 1tp4_validation.xml.gz | 45.2 KB | Display | |
Data in CIF | 1tp4_validation.cif.gz | 67.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/tp/1tp4 ftp://data.pdbj.org/pub/pdb/validation_reports/tp/1tp4 | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 10782.896 Da / Num. of mol.: 1 / Fragment: XPC binding domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: RAD23A / Plasmid: pGEX2T / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: P54725 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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NMR details | Text: The structure was determined using triple-resonance NMR spectroscopy. |
-Sample preparation
Details | Contents: 1mM XPCB U-15N,13C, 20mM sodium phosphate, 122mM sodium chloride, 0.05% sodium azide Solvent system: 95% H2O/5% D2O |
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Sample conditions | Ionic strength: 20mM sodium phosphate, 122mM sodium chloride, 0.05% sodium azide pH: 7.3 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz |
-Processing
NMR software |
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Refinement | Method: distance geometry / Software ordinal: 1 Details: The structures are based on a total of 917 non-redundant NOE-derived distance constraints, 82 dihedral angle restraints and 42 distance restraints from hydrogen bonds. | |||||||||||||||
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: 25 |