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Open data
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Basic information
Entry | Database: PDB / ID: 6k2k | ||||||
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Title | Solution structure of MUL1-RING domain | ||||||
![]() | Mitochondrial ubiquitin ligase activator of NFKB 1 | ||||||
![]() | STRUCTURAL PROTEIN / Solution structure / E3 ubiquitin ligase | ||||||
Function / homology | ![]() regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway / negative regulation of chemokine (C-C motif) ligand 5 production / negative regulation of defense response to virus by host / negative regulation of mitochondrial fusion / mitochondrion localization / positive regulation of protein sumoylation / positive regulation of dendrite extension / positive regulation of type 2 mitophagy / mitochondrial fission / regulation of mitochondrion organization ...regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway / negative regulation of chemokine (C-C motif) ligand 5 production / negative regulation of defense response to virus by host / negative regulation of mitochondrial fusion / mitochondrion localization / positive regulation of protein sumoylation / positive regulation of dendrite extension / positive regulation of type 2 mitophagy / mitochondrial fission / regulation of mitochondrion organization / SUMO transferase activity / negative regulation of type I interferon-mediated signaling pathway / positive regulation of mitochondrial fission / cellular response to exogenous dsRNA / protein sumoylation / negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / negative regulation of innate immune response / regulation of mitochondrial membrane potential / : / negative regulation of cell growth / protein destabilization / RING-type E3 ubiquitin transferase / protein polyubiquitination / ubiquitin-protein transferase activity / KEAP1-NFE2L2 pathway / ubiquitin protein ligase activity / p53 binding / peroxisome / Neddylation / positive regulation of canonical NF-kappaB signal transduction / mitochondrial outer membrane / protein stabilization / Ub-specific processing proteases / protein ubiquitination / axon / neuronal cell body / apoptotic process / ubiquitin protein ligase binding / mitochondrion / identical protein binding / membrane / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
![]() | Lee, M.S. / Lee, M.K. / Ryu, K.S. / Chi, S.W. | ||||||
![]() | ![]() Title: Solution structure of MUL1-RING domain and its interaction with p53 transactivation domain. Authors: Lee, M.S. / Lee, S.O. / Lee, M.K. / Yi, G.S. / Lee, C.K. / Ryu, K.S. / Chi, S.W. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 384.2 KB | Display | ![]() |
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PDB format | ![]() | 323.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 530.6 KB | Display | ![]() |
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Full document | ![]() | 637 KB | Display | |
Data in XML | ![]() | 23.4 KB | Display | |
Data in CIF | ![]() | 38.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-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: 6251.479 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q969V5, RING-type E3 ubiquitin transferase |
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#2: Chemical |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Details | Type: solution Contents: 0.9 mM [U-99% 13C; U-99% 15N] Mitochondrial ubiquitin ligase activator of NFKB 1, 90% H2O/10% D2O Details: 13C, 15N-labeled MUL1-RING domain / Label: 13C, 15N_sample / Solvent system: 90% H2O/10% D2O |
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Sample | Conc.: 0.9 mM Component: Mitochondrial ubiquitin ligase activator of NFKB 1 Isotopic labeling: [U-99% 13C; U-99% 15N] |
Sample conditions | Details: 50 mM MES, pH 6.5, 50 mM NaCl, 5 microM Zinc sulfate, 10 mM dithiothreitol (DTT), and 10 % (v/v) D2O Ionic strength: 50 mM / Label: conditions_1 / pH: 6.5 / Pressure: 1 atm / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE II / Manufacturer: Bruker / Model: AVANCE II / Field strength: 900 MHz |
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Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||||
NMR representative | Selection criteria: minimized average structure | ||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 250 / Conformers submitted total number: 20 |