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Yorodumi- PDB-6sjz: HsNMT1 in complex with both MyrCoA and Acetylated-GNCFSKPR substrates -
+Open data
-Basic information
Entry | Database: PDB / ID: 6sjz | ||||||||||||
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Title | HsNMT1 in complex with both MyrCoA and Acetylated-GNCFSKPR substrates | ||||||||||||
Components |
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Keywords | TRANSFERASE / NMT / MYRISTOYLTRANSFERASE TYPE1 / ACYLTRANSFERASE / GNAT / GCN5-RELATED N-ACETYLTRANSFERASES | ||||||||||||
Function / homology | Function and homology information 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 / Oxidoreductases / oxidoreductase activity, acting on NAD(P)H / execution phase of apoptosis / Transferases; Acyltransferases; Transferring groups other than aminoacyl groups / 2 iron, 2 sulfur cluster binding / Inactivation, recovery and regulation of the phototransduction cascade / flavin adenine dinucleotide binding / mitochondrial inner membrane / in utero embryonic development / endoplasmic reticulum / mitochondrion / metal ion binding / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||||||||
Biological species | Homo sapiens (human) | ||||||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.995 Å | ||||||||||||
Authors | Dian, C. / Riviere, F.B. / Asensio, T. / Giglione, C. / Meinnel, T. | ||||||||||||
Funding support | France, 3items
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Citation | Journal: Nat Commun / Year: 2020 Title: High-resolution snapshots of human N-myristoyltransferase in action illuminate a mechanism promoting N-terminal Lys and Gly myristoylation. Authors: Dian, C. / Perez-Dorado, I. / Riviere, F. / Asensio, T. / Legrand, P. / Ritzefeld, M. / Shen, M. / Cota, E. / Meinnel, T. / Tate, E.W. / Giglione, C. | ||||||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6sjz.cif.gz | 195.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6sjz.ent.gz | 151.3 KB | Display | PDB format |
PDBx/mmJSON format | 6sjz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/sj/6sjz ftp://data.pdbj.org/pub/pdb/validation_reports/sj/6sjz | HTTPS FTP |
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-Related structure data
Related structure data | 6ehjC 6qrmC 6sk2C 6sk3C 6sk8C 6skjC 5o9vS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
-Protein / Protein/peptide , 2 types, 4 molecules ABEF
#1: Protein | Mass: 46465.414 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: NMT1, NMT / Plasmid: pET28 derivative / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): Rosetta2 pLysS References: UniProt: P30419, glycylpeptide N-tetradecanoyltransferase #2: Protein/peptide | Mass: 936.090 Da / Num. of mol.: 2 / Mutation: G3N, P8R / Source method: obtained synthetically / Details: Acetylated peptide / Source: (synth.) Homo sapiens (human) / References: UniProt: Q96NN9, Oxidoreductases |
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-Non-polymers , 4 types, 604 molecules
#3: Chemical | #4: Chemical | #5: Chemical | ChemComp-GOL / #6: Water | ChemComp-HOH / | |
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-Details
Has ligand of interest | Y |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.2 Å3/Da / Density % sol: 44.16 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 5.5 Details: 22% PEG6K, 100mM Sodium Citrate pH 5.5, 100mM MgCl2, 100mM NaCl. |
-Data collection
Diffraction | Mean temperature: 100 K / Ambient temp details: 100 K cryostream / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: MASSIF-1 / Wavelength: 0.966 Å |
Detector | Type: DECTRIS PILATUS3 2M / Detector: PIXEL / Date: Jun 8, 2016 |
Radiation | Monochromator: Laue [110] diamond / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.966 Å / Relative weight: 1 |
Reflection | Resolution: 1.99→48.89 Å / Num. obs: 115590 / % possible obs: 99.5 % / Redundancy: 8 % / Biso Wilson estimate: 21.32 Å2 / CC1/2: 0.998 / Rmerge(I) obs: 0.103 / Rpim(I) all: 0.038 / Rrim(I) all: 0.11 / Net I/σ(I): 14.4 |
Reflection shell | Resolution: 1.99→2.05 Å / Redundancy: 6.8 % / Rmerge(I) obs: 0.509 / Num. unique obs: 3937 / CC1/2: 0.897 / Rpim(I) all: 0.203 / Rrim(I) all: 0.55 / % possible all: 93.6 |
-Phasing
Phasing | Method: molecular replacement | ||||||
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Phasing MR | R rigid body: 0.36
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 5O9V Resolution: 1.995→48.888 Å / SU ML: 0.17 / Cross valid method: THROUGHOUT / σ(F): 0.01 / Phase error: 19.4
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 86.17 Å2 / Biso mean: 27.1155 Å2 / Biso min: 7.38 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 1.995→48.888 Å
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Refine LS restraints |
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LS refinement shell |
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