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Open data
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Basic information
Entry | Database: PDB / ID: 2my9 | ||||||
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Title | Solution structure of N-terminal domain of human TIG3 | ||||||
![]() | Retinoic acid receptor responder protein 3 | ||||||
![]() | HYDROLASE / TIG3 / H-REV107 family / NlpC/P60 / phospholipase | ||||||
Function / homology | ![]() positive regulation of protein-glutamine gamma-glutamyltransferase activity / phosphatidylethanolamine acyl-chain remodeling / N-acylphosphatidylethanolamine metabolic process / phospholipase A1 / phosphatidylserine 1-acylhydrolase activity / 1-acyl-2-lysophosphatidylserine acylhydrolase activity / phospholipase A1 activity / Acyl chain remodelling of PE / N-acyltransferase activity / phospholipase A2 activity ...positive regulation of protein-glutamine gamma-glutamyltransferase activity / phosphatidylethanolamine acyl-chain remodeling / N-acylphosphatidylethanolamine metabolic process / phospholipase A1 / phosphatidylserine 1-acylhydrolase activity / 1-acyl-2-lysophosphatidylserine acylhydrolase activity / phospholipase A1 activity / Acyl chain remodelling of PE / N-acyltransferase activity / phospholipase A2 activity / positive regulation of keratinocyte differentiation / phospholipase A2 / acyltransferase activity / phospholipid metabolic process / lipid catabolic process / Transferases; Acyltransferases; Transferring groups other than aminoacyl groups / negative regulation of cell population proliferation / membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / DGSA-distance geometry simulated annealing | ||||||
Model details | lowest energy, model1 | ||||||
![]() | Wei, H. / Wang, L. / Xia, B. | ||||||
![]() | ![]() Title: Structural and functional characterization of tumor suppressors TIG3 and H-REV107. Authors: Wei, H. / Wang, L. / Ren, X. / Yu, W. / Lin, J. / Jin, C. / Xia, B. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 763.8 KB | Display | ![]() |
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PDB format | ![]() | 643.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 407.5 KB | Display | ![]() |
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Full document | ![]() | 502.1 KB | Display | |
Data in XML | ![]() | 35.1 KB | Display | |
Data in CIF | ![]() | 62.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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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 | Mass: 14050.886 Da / Num. of mol.: 1 / Fragment: N-terminal domain (UNP residues 1-125) Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q9UL19, Hydrolases; Acting on ester bonds; Carboxylic-ester hydrolases |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Details | Contents: 0.5 mM [U-13C; U-15N] TIG3N, 0.03% DSS, 20 mM DTT, 50 mM sodium chloride, 50 mM potassium chloride, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 100 / pH: 7.0 / Pressure: ambient / Temperature: 308 K |
-NMR measurement
NMR spectrometer |
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Processing
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Refinement | Method: DGSA-distance geometry simulated annealing / Software ordinal: 1 | ||||||||||||||||||||||||||||||||||||||||||||
NMR constraints | NOE constraints total: 3510 / NOE intraresidue total count: 1360 / NOE long range total count: 532 / NOE medium range total count: 281 / NOE sequential total count: 586 / Hydrogen bond constraints total count: 6 / Protein other angle constraints total count: 439 / Protein phi angle constraints total count: 63 / Protein psi angle constraints total count: 62 | ||||||||||||||||||||||||||||||||||||||||||||
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: 20 |