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Open data
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Basic information
Entry | Database: PDB / ID: 2n9e | ||||||
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Title | Structure of SUMO-2 bound to phosphorylated RAP80 SIM | ||||||
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![]() | PROTEIN BINDING / SUMO-2-phosphoRAP80 / SUMO-2-phosphoSIM | ||||||
Function / homology | ![]() BRCA1-A complex / ubiquitin-modified histone reader activity / 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 / mitotic G2/M transition checkpoint / SUMOylation of RNA binding proteins / DNA repair-dependent chromatin remodeling ...BRCA1-A complex / ubiquitin-modified histone reader activity / 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 / mitotic G2/M transition checkpoint / SUMOylation of RNA binding proteins / DNA repair-dependent chromatin remodeling / K63-linked polyubiquitin modification-dependent protein binding / response to ionizing radiation / ubiquitin-like protein ligase binding / mitotic G2 DNA damage checkpoint signaling / SUMOylation of DNA replication proteins / SUMOylation of transcription factors / protein sumoylation / regulation of DNA repair / SUMOylation of DNA damage response and repair proteins / positive regulation of DNA repair / SUMOylation of chromatin organization proteins / SUMOylation of transcription cofactors / Nonhomologous End-Joining (NHEJ) / SUMOylation of intracellular receptors / G2/M DNA damage checkpoint / Metalloprotease DUBs / PML body / Formation of Incision Complex in GG-NER / protein tag activity / double-strand break repair / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / 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 / ubiquitin protein ligase binding / DNA binding / RNA binding / nucleoplasm / nucleus / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / molecular dynamics, torsion angle dynamics | ||||||
![]() | Anamika, A. / Spyracopoulos, L. | ||||||
![]() | ![]() Title: Molecular Basis for Phosphorylation-dependent SUMO Recognition by the DNA Repair Protein RAP80. Authors: Anamika / Spyracopoulos, L. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 672.3 KB | Display | ![]() |
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PDB format | ![]() | 585.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 427 KB | Display | ![]() |
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Full document | ![]() | 642.4 KB | Display | |
Data in XML | ![]() | 44.3 KB | Display | |
Data in CIF | ![]() | 69 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar 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: 1580.415 Da / Num. of mol.: 1 / Fragment: SUMO interacting motif (UNP residues 37-49) / Source method: obtained synthetically / Source: (synth.) ![]() |
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#2: Protein | Mass: 10886.217 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Details | Contents: 1.2 mM peptide, 0.4 mM [U-100% 13C; U-100% 15N] protein, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||
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Sample |
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Sample conditions | Ionic strength: 25 / pH: 7.3 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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Processing
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Refinement | Method: molecular dynamics, torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||
NMR constraints | NOE constraints total: 45 / NOE intraresidue total count: 3 / NOE long range total count: 0 / NOE medium range total count: 6 / NOE sequential total count: 21 / Protein chi angle constraints total count: 30 / Protein other angle constraints total count: 0 / Protein phi angle constraints total count: 68 / Protein psi angle constraints total count: 68 | ||||||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 20 / Conformers submitted total number: 20 / Maximum lower distance constraint violation: 0 Å / Maximum upper distance constraint violation: 0 Å | ||||||||||||||||||||||||
NMR ensemble rms | Distance rms dev: 0 Å / Distance rms dev error: 2 Å |