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Yorodumi- PDB-4ay5: Human O-GlcNAc transferase (OGT) in complex with UDP and glycopeptide -
+Open data
-Basic information
Entry | Database: PDB / ID: 4ay5 | ||||||
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Title | Human O-GlcNAc transferase (OGT) in complex with UDP and glycopeptide | ||||||
Components |
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Keywords | TRANSFERASE/PEPTIDE / TRANSFERASE-PEPTIDE COMPLEX / TRANSFERASE / GLYCOSYL TRANSFERASE / TRIMERIC PRODUCT COMPLEX / O-GLCNAC | ||||||
Function / homology | Function and homology information protein N-acetylglucosaminyltransferase complex / protein O-GlcNAc transferase / regulation of insulin receptor signaling pathway / protein O-acetylglucosaminyltransferase activity / positive regulation of transcription from RNA polymerase II promoter by glucose / cardiac septum development / acetylglucosaminyltransferase activity / regulation of necroptotic process / regulation of Rac protein signal transduction / negative regulation of stem cell population maintenance ...protein N-acetylglucosaminyltransferase complex / protein O-GlcNAc transferase / regulation of insulin receptor signaling pathway / protein O-acetylglucosaminyltransferase activity / positive regulation of transcription from RNA polymerase II promoter by glucose / cardiac septum development / acetylglucosaminyltransferase activity / regulation of necroptotic process / regulation of Rac protein signal transduction / negative regulation of stem cell population maintenance / protein O-linked glycosylation / coronary vasculature development / NSL complex / : / aorta development / regulation of neurotransmitter receptor localization to postsynaptic specialization membrane / regulation of glycolytic process / RIPK1-mediated regulated necrosis / regulation of synapse assembly / regulation of gluconeogenesis / protein serine/threonine phosphatase activity / mitogen-activated protein kinase p38 binding / positive regulation of stem cell population maintenance / Formation of WDR5-containing histone-modifying complexes / non-canonical NF-kappaB signal transduction / positive regulation of proteolysis / phosphatidylinositol-3,4,5-trisphosphate binding / mitophagy / hemopoiesis / enzyme activator activity / negative regulation of proteasomal ubiquitin-dependent protein catabolic process / histone acetyltransferase complex / positive regulation of lipid biosynthetic process / heart morphogenesis / negative regulation of protein ubiquitination / IRAK2 mediated activation of TAK1 complex / Alpha-protein kinase 1 signaling pathway / IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation / TICAM1,TRAF6-dependent induction of TAK1 complex / positive regulation of TORC1 signaling / TRAF6-mediated induction of TAK1 complex within TLR4 complex / protein serine/threonine kinase activator activity / response to nutrient / transforming growth factor beta receptor signaling pathway / negative regulation of cell migration / JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 / positive regulation of translation / TNFR1-induced NF-kappa-B signaling pathway / cell projection / activated TAK1 mediates p38 MAPK activation / cellular response to glucose stimulus / mitochondrial membrane / lung development / negative regulation of transforming growth factor beta receptor signaling pathway / circadian regulation of gene expression / TAK1-dependent IKK and NF-kappa-B activation / response to insulin / NOD1/2 Signaling Pathway / positive regulation of protein serine/threonine kinase activity / Regulation of necroptotic cell death / chromatin DNA binding / protein processing / CLEC7A (Dectin-1) signaling / FCERI mediated NF-kB activation / Interleukin-1 signaling / UCH proteinases / chromatin organization / positive regulation of cold-induced thermogenesis / HATs acetylate histones / in utero embryonic development / positive regulation of MAPK cascade / molecular adaptor activity / endosome membrane / Ub-specific processing proteases / nuclear speck / glutamatergic synapse / apoptotic process / protein-containing complex binding / regulation of transcription by RNA polymerase II / SARS-CoV-2 activates/modulates innate and adaptive immune responses / positive regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II / endoplasmic reticulum / signal transduction / positive regulation of transcription by RNA polymerase II / protein-containing complex / nucleoplasm / nucleus / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | HOMO SAPIENS (human) SYNTHETIC CONSTRUCT (others) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / OTHER / Resolution: 3.15 Å | ||||||
Authors | Schimpl, M. / Zheng, X. / Blair, D.E. / Schuettelkopf, A.W. / Navratilova, I. / Aristotelous, T. / Ferenbach, A.T. / Macnaughtan, M.A. / Borodkin, V.S. / van Aalten, D.M.F. | ||||||
Citation | Journal: Nat.Chem.Biol. / Year: 2012 Title: O-Glcnac Transferase Invokes Nucleotide Sugar Pyrophosphate Participation in Catalysis Authors: Schimpl, M. / Zheng, X. / Borodkin, V.S. / Blair, D.E. / Ferenbach, A.T. / Schuettelkopf, A.W. / Navratilova, I. / Aristotelous, T. / Albarbarawi, O. / Robinson, D.A. / Macnaughtan, M.A. / Van Aalten, D.M.F. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4ay5.cif.gz | 548.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4ay5.ent.gz | 454.3 KB | Display | PDB format |
PDBx/mmJSON format | 4ay5.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ay/4ay5 ftp://data.pdbj.org/pub/pdb/validation_reports/ay/4ay5 | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
NCS oper:
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-Components
#1: Protein | Mass: 80974.508 Da / Num. of mol.: 4 Fragment: TPR (TRUNCATED) AND CATALYTIC DOMAIN, RESIDUES 313-1031 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PGEX6P1 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 / Variant (production host): ARCTICEXPRESS (RIL) / References: UniProt: O15294, protein O-GlcNAc transferase #2: Protein/peptide | Mass: 1121.198 Da / Num. of mol.: 4 / Source method: obtained synthetically / Source: (synth.) SYNTHETIC CONSTRUCT (others) / References: UniProt: Q15750*PLUS #3: Chemical | ChemComp-UDP / #4: Sugar | ChemComp-NAG / Sequence details | CHAINS I, J, K, AND L ARE GTAB1TIDE, A SYNTHETIC GLYCOPEPTIDE BASED ON RESIDUES 389-399 OF HUMAN ...CHAINS I, J, K, AND L ARE GTAB1TIDE, A SYNTHETIC GLYCOPEPTI | |
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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: 4.7 Å3/Da / Density % sol: 73.81 % / Description: NONE |
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Crystal grow | pH: 9.3 / Details: 1.45 M K2HPO4, 10 MM EDTA, 1% XYLITOL, pH 9.3 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-4 / Wavelength: 0.939 |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: May 1, 2011 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.939 Å / Relative weight: 1 |
Reflection | Resolution: 3.15→30 Å / Num. obs: 105108 / % possible obs: 99.7 % / Observed criterion σ(I): 2 / Redundancy: 3.6 % / Rmerge(I) obs: 0.11 / Net I/σ(I): 6.7 |
-Processing
Software | Name: REFMAC / Version: 5.6.0117 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Method to determine structure: OTHER Starting model: NONE Resolution: 3.15→237.44 Å / Cor.coef. Fo:Fc: 0.947 / Cor.coef. Fo:Fc free: 0.925 / SU B: 13.759 / SU ML: 0.223 / Cross valid method: THROUGHOUT / ESU R: 0.673 / ESU R Free: 0.298 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. RESIDUES 715-718 AND 747-761 ARE DISORDERED.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 60.844 Å2
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Refinement step | Cycle: LAST / Resolution: 3.15→237.44 Å
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