+Open data
-Basic information
Entry | Database: PDB / ID: 2mkg | ||||||
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Title | Solution structure of the tandem UIMs of RAP80 | ||||||
Components | BRCA1-A complex subunit RAP80 | ||||||
Keywords | SIGNALING PROTEIN / UIM / Ubiquitin-interacting motif / DNA damage response | ||||||
Function / homology | Function and homology information BRCA1-A complex / ubiquitin-modified histone reader activity / mitotic G2/M transition checkpoint / DNA repair-dependent chromatin remodeling / K63-linked polyubiquitin modification-dependent protein binding / response to ionizing radiation / mitotic G2 DNA damage checkpoint signaling / regulation of DNA repair / positive regulation of DNA repair / Nonhomologous End-Joining (NHEJ) ...BRCA1-A complex / ubiquitin-modified histone reader activity / mitotic G2/M transition checkpoint / DNA repair-dependent chromatin remodeling / K63-linked polyubiquitin modification-dependent protein binding / response to ionizing radiation / mitotic G2 DNA damage checkpoint signaling / regulation of DNA repair / positive regulation of DNA repair / Nonhomologous End-Joining (NHEJ) / G2/M DNA damage checkpoint / Metalloprotease DUBs / double-strand break repair / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / site of double-strand break / Processing of DNA double-strand break ends / histone binding / nuclear body / negative regulation of DNA-templated transcription / DNA binding / nucleoplasm / metal ion binding / nucleus Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR | ||||||
Model details | closest to the average, model6 | ||||||
Authors | Anamika / Markin, C.J. / Rout, M.K. / Spyracopoulos, L. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2014 Title: Molecular Basis for Impaired DNA Damage Response Function Associated with the RAP80 Delta E81 Defect. Authors: Anamika / Markin, C.J. / Rout, M.K. / Spyracopoulos, L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2mkg.cif.gz | 377.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2mkg.ent.gz | 319.6 KB | Display | PDB format |
PDBx/mmJSON format | 2mkg.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mk/2mkg ftp://data.pdbj.org/pub/pdb/validation_reports/mk/2mkg | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 7018.696 Da / Num. of mol.: 1 / Fragment: UIM 1-2 (UNP residues 74-131) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: UIMC1, RAP80, RXRIP110 / Plasmid: pGEX-6P1 / Production host: Escherichia coli (E. coli) / References: UniProt: Q96RL1 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample |
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Sample conditions | Ionic strength: 150 / pH: 7.3 / Pressure: ambient / Temperature: 278 K |
-NMR measurement
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz |
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-Processing
NMR software |
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NMR constraints | NOE constraints total: 65 / NOE intraresidue total count: 24 / NOE medium range total count: 1 / NOE sequential total count: 40 / Protein chi angle constraints total count: 15 / Protein phi angle constraints total count: 57 / Protein psi angle constraints total count: 57 | |||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | |||||||||||||||||||||
NMR ensemble | Conformer selection criteria: all calculated structures submitted Conformers calculated total number: 20 / Conformers submitted total number: 20 |