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Yorodumi- PDB-1e32: Structure of the N-Terminal domain and the D1 AAA domain of membr... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1.0E+32 | ||||||
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Title | Structure of the N-Terminal domain and the D1 AAA domain of membrane fusion ATPase p97 | ||||||
Components | P97 | ||||||
Keywords | ATPASE / MEMBRANE FUSION | ||||||
Function / homology | Function and homology information RHOH GTPase cycle / HSF1 activation / Protein methylation / Translesion Synthesis by POLH / Josephin domain DUBs / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / Ovarian tumor domain proteases / Hedgehog ligand biogenesis / KEAP1-NFE2L2 pathway / ABC-family proteins mediated transport ...RHOH GTPase cycle / HSF1 activation / Protein methylation / Translesion Synthesis by POLH / Josephin domain DUBs / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / Ovarian tumor domain proteases / Hedgehog ligand biogenesis / KEAP1-NFE2L2 pathway / ABC-family proteins mediated transport / Neddylation / flavin adenine dinucleotide catabolic process / positive regulation of oxidative phosphorylation / VCP-NSFL1C complex / protein-DNA covalent cross-linking repair / endosome to lysosome transport via multivesicular body sorting pathway / positive regulation of ubiquitin-dependent protein catabolic process / endoplasmic reticulum stress-induced pre-emptive quality control / cellular response to arsenite ion / BAT3 complex binding / Derlin-1 retrotranslocation complex / positive regulation of protein K63-linked deubiquitination / deubiquitinase activator activity / mitotic spindle disassembly / VCP-NPL4-UFD1 AAA ATPase complex / aggresome assembly / regulation of protein localization to chromatin / NADH metabolic process / vesicle-fusing ATPase / : / positive regulation of mitochondrial membrane potential / stress granule disassembly / K48-linked polyubiquitin modification-dependent protein binding / negative regulation of protein localization to chromatin / ERAD pathway / ubiquitin-modified protein reader activity / retrograde protein transport, ER to cytosol / regulation of aerobic respiration / ATPase complex / regulation of synapse organization / positive regulation of ATP biosynthetic process / ubiquitin-specific protease binding / ubiquitin-like protein ligase binding / autophagosome maturation / polyubiquitin modification-dependent protein binding / translesion synthesis / endoplasmic reticulum to Golgi vesicle-mediated transport / MHC class I protein binding / interstrand cross-link repair / negative regulation of smoothened signaling pathway / ATP metabolic process / : / Neutrophil degranulation / proteasome complex / lipid droplet / viral genome replication / ADP binding / proteasomal protein catabolic process / positive regulation of protein-containing complex assembly / macroautophagy / autophagy / cytoplasmic stress granule / positive regulation of non-canonical NF-kappaB signal transduction / positive regulation of canonical Wnt signaling pathway / positive regulation of protein catabolic process / double-strand break repair / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / site of double-strand break / myelin sheath / cellular response to heat / ubiquitin-dependent protein catabolic process / proteasome-mediated ubiquitin-dependent protein catabolic process / protein phosphatase binding / protein ubiquitination / protein domain specific binding / DNA repair / lipid binding / glutamatergic synapse / synapse / DNA damage response / ubiquitin protein ligase binding / protein-containing complex binding / endoplasmic reticulum membrane / perinuclear region of cytoplasm / endoplasmic reticulum / ATP hydrolysis activity / protein-containing complex / nucleoplasm / ATP binding / identical protein binding / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | MUS MUSCULUS (house mouse) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MIRAS / Resolution: 2.9 Å | ||||||
Authors | Zhang, X. / Shaw, A. / Bates, P.A. / Gorman, M.A. / Kondo, H. / Dokurno, P. / Leonard M, G. / Sternberg, J.E. / Freemont, P.S. | ||||||
Citation | Journal: Mol.Cell / Year: 2000 Title: Structure of the Aaa ATPase P97 Authors: Zhang, X. / Shaw, A. / Bates, P.A. / Newman, R.H. / Gowen, B. / Orlova, E. / Gorman, M.A. / Kondo, H. / Dokurno, P. / Lally, J. / Leonard, G. / Meyer, H. / Van Heel, M. / Freemont, P.S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1e32.cif.gz | 93.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1e32.ent.gz | 74.8 KB | Display | PDB format |
PDBx/mmJSON format | 1e32.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/e3/1e32 ftp://data.pdbj.org/pub/pdb/validation_reports/e3/1e32 | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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Unit cell |
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-Components
#1: Protein | Mass: 51027.477 Da / Num. of mol.: 1 Fragment: N TERMINAL DOMAIN AND D1 AAA DOMAIN, RESIDUES 1-458 Source method: isolated from a genetically manipulated source Source: (gene. exp.) MUS MUSCULUS (house mouse) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): ER2566 / References: UniProt: Q01853 |
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#2: Chemical | ChemComp-ADP / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.56 Å3/Da / Density % sol: 55 % | |||||||||||||||||||||||||
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Crystal grow | pH: 6 Details: 3.8-4.2 M NAFORMATE, 10% GLYCEROL, 5% PEG600, PH 5.5-6.0 | |||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop / PH range low: 6 / PH range high: 5.5 | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: X11 / Wavelength: 0.9 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Sep 15, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9 Å / Relative weight: 1 |
Reflection | Resolution: 2.9→30 Å / Num. obs: 12114 / % possible obs: 99.8 % / Observed criterion σ(I): 2 / Redundancy: 19 % / Biso Wilson estimate: 39.9 Å2 / Rmerge(I) obs: 0.09 / Rsym value: 0.09 / Net I/σ(I): 9.7 |
Reflection shell | Resolution: 2.9→3 Å / Redundancy: 15 % / Rmerge(I) obs: 0.3 / % possible all: 100 |
Reflection | *PLUS Lowest resolution: 30 Å / Redundancy: 19.3 % / Rmerge(I) obs: 0.09 |
Reflection shell | *PLUS Rmerge(I) obs: 0.3 |
-Processing
Software |
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Refinement | Method to determine structure: MIRAS / Resolution: 2.9→15 Å / Rfactor Rfree error: 0.008 / Data cutoff high absF: 10000 / Cross valid method: THROUGHOUT / σ(F): 2 Details: RES 337 AND 338 HAVE ZERO OCCUPACIES AND REGIONS BETWEEN 312-317, 432-437 HAVE POOR ELECTRON DENSITI
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 33 Å2 / ksol: 0.33 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 33 Å2
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Refinement step | Cycle: LAST / Resolution: 2.9→15 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.9→3.03 Å / Rfactor Rfree error: 0.034 / Total num. of bins used: 8 /
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