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- PDB-7owq: HsNMT1 in complex with both MyrCoA and peptide N-Methylated-GNCFSKPR -
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Open data
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Basic information
Entry | Database: PDB / ID: 7owq | ||||||||||||
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Title | HsNMT1 in complex with both MyrCoA and peptide N-Methylated-GNCFSKPR | ||||||||||||
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![]() | TRANSFERASE / N-MYRISTOYLATION / NMT / MYRISTOYLTRANSFERASE TYPE1 / ACYLTRANSFERASE / GNAT / GCN5-RELATED N-ACETYLTRANSFERASES | ||||||||||||
Function / homology | ![]() myristoyltransferase activity / peptidyl-lysine N6-myristoyltransferase activity / N-terminal peptidyl-glycine N-myristoylation / Late Phase of HIV Life Cycle / cellular ketone metabolic process / regulation of opsin-mediated signaling pathway / Activation, myristolyation of BID and translocation to mitochondria / glycylpeptide N-tetradecanoyltransferase / glycylpeptide N-tetradecanoyltransferase activity / protein localization to membrane ...myristoyltransferase activity / peptidyl-lysine N6-myristoyltransferase activity / N-terminal peptidyl-glycine N-myristoylation / Late Phase of HIV Life Cycle / cellular ketone metabolic process / regulation of opsin-mediated signaling pathway / Activation, myristolyation of BID and translocation to mitochondria / glycylpeptide N-tetradecanoyltransferase / glycylpeptide N-tetradecanoyltransferase activity / protein localization to membrane / Transferases; Acyltransferases; Transferring groups other than aminoacyl groups / Inactivation, recovery and regulation of the phototransduction cascade / in utero embryonic development / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||||||||
Biological species | ![]() | ||||||||||||
Method | ![]() ![]() ![]() | ||||||||||||
![]() | Dian, C. / Giglione, C. / Meinnel, T. | ||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural and Large-scale Analysis Unveil the Intertwined Paths Promoting NMT-catalyzed Lysine and Glycine Myristoylation. Authors: Riviere, F. / Dian, C. / Dutheil, R.F. / Monassa, P. / Giglione, C. / Meinnel, T. | ||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 211.2 KB | Display | ![]() |
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PDB format | ![]() | 134 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 814.6 KB | Display | ![]() |
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Full document | ![]() | 824.8 KB | Display | |
Data in XML | ![]() | 30.7 KB | Display | |
Data in CIF | ![]() | 40 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7owmC ![]() 7ownC ![]() 7owoC ![]() 7owpC ![]() 7owrC ![]() 7owuC ![]() 5o9vS S: Starting model for refinement C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 46465.414 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P30419, glycylpeptide N-tetradecanoyltransferase #2: Protein/peptide | Mass: 924.079 Da / Num. of mol.: 2 / Source method: obtained synthetically / Details: N-acetylated-Glycine-peptide / Source: (synth.) ![]() #3: Chemical | Has ligand of interest | Y | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.24 Å3/Da / Density % sol: 45.12 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 5.6 Details: 21% PEG 8K, 0.1M sodum citrate, 0.1 M MgCl2, 0.2M NaCl |
-Data collection
Diffraction | Mean temperature: 100 K / Ambient temp details: Cryostream / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS EIGER R 4M / Detector: PIXEL / Date: Feb 8, 2016 |
Radiation | Monochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.96775 Å / Relative weight: 1 |
Reflection | Resolution: 3→47.69 Å / Num. obs: 32321 / % possible obs: 98.6 % / Redundancy: 6.3 % / Biso Wilson estimate: 49.82 Å2 / CC1/2: 0.993 / Rpim(I) all: 0.058 / Rsym value: 0.134 / Net I/σ(I): 11.2 |
Reflection shell | Resolution: 3→3.18 Å / Redundancy: 5.9 % / Mean I/σ(I) obs: 3 / Num. unique obs: 2710 / CC1/2: 0.856 / Rpim(I) all: 0.265 / Rsym value: 0.601 / % possible all: 98.7 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 5O9V Resolution: 3→47.69 Å / SU ML: 0.4087 / Cross valid method: FREE R-VALUE / σ(F): 0.37 / Phase error: 27.5367 Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 45.33 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3→47.69 Å
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Refine LS restraints |
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LS refinement shell |
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