+Open data
-Basic information
Entry | Database: PDB / ID: 1hhn | ||||||
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Title | Calreticulin P-domain | ||||||
Components | CALRETICULIN | ||||||
Keywords | MOLECULAR CHAPERONE | ||||||
Function / homology | Function and homology information Scavenging by Class A Receptors / Calnexin/calreticulin cycle / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / ER-Phagosome pathway / cytolytic granule / positive regulation of dendritic cell chemotaxis / cortical granule / negative regulation of trophoblast cell migration / negative regulation of retinoic acid receptor signaling pathway / complement component C1q complex binding ...Scavenging by Class A Receptors / Calnexin/calreticulin cycle / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / ER-Phagosome pathway / cytolytic granule / positive regulation of dendritic cell chemotaxis / cortical granule / negative regulation of trophoblast cell migration / negative regulation of retinoic acid receptor signaling pathway / complement component C1q complex binding / endoplasmic reticulum quality control compartment / cellular response to electrical stimulus / regulation of meiotic nuclear division / response to glycoside / sarcoplasmic reticulum lumen / hormone binding / nuclear export signal receptor activity / negative regulation of intracellular steroid hormone receptor signaling pathway / cardiac muscle cell differentiation / molecular sequestering activity / cortical actin cytoskeleton organization / nuclear androgen receptor binding / : / response to testosterone / cellular response to lithium ion / ERAD pathway / protein localization to nucleus / negative regulation of neuron differentiation / smooth endoplasmic reticulum / positive regulation of cell cycle / positive regulation of substrate adhesion-dependent cell spreading / positive regulation of phagocytosis / protein export from nucleus / positive regulation of endothelial cell migration / : / acrosomal vesicle / sarcoplasmic reticulum / peptide binding / peptide antigen assembly with MHC class I protein complex / MHC class I peptide loading complex / cellular response to virus / positive regulation of non-canonical NF-kappaB signal transduction / cellular senescence / unfolded protein binding / integrin binding / protein folding / response to estradiol / nuclear envelope / spermatogenesis / carbohydrate binding / collagen-containing extracellular matrix / negative regulation of translation / protein stabilization / ribosome / response to xenobiotic stimulus / iron ion binding / external side of plasma membrane / endoplasmic reticulum lumen / negative regulation of DNA-templated transcription / mRNA binding / ubiquitin protein ligase binding / calcium ion binding / positive regulation of cell population proliferation / endoplasmic reticulum membrane / positive regulation of gene expression / perinuclear region of cytoplasm / negative regulation of transcription by RNA polymerase II / cell surface / endoplasmic reticulum / protein-containing complex / extracellular space / membrane / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | RATTUS NORVEGICUS (Norway rat) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Ellgaard, L. / Riek, R. / Herrmann, T. / Guntert, P. / Braun, D. / Helenius, A. / Wuthrich, K. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2001 Title: NMR Structure of the Calreticulin P-Domain Authors: Ellgaard, L. / Riek, R. / Herrmann, T. / Braun, D. / Guntert, P. / Helenius, A. / Wuthrich, K. #1: Journal: FEBS Lett. / Year: 2000 Title: Three-Dimensional Structure Topology of the Calreticulin P-Domain Based on NMR Assignment Authors: Ellgaard, L. / Riek, R. / Braun, D. / Herrmann, T. / Helenius, A. / Wuthrich, K. | ||||||
History |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR PROVIDED. | ||||||
Remark 700 | SHEET DETERMINATION METHOD: AUTHOR PROVIDED. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1hhn.cif.gz | 622.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1hhn.ent.gz | 519.7 KB | Display | PDB format |
PDBx/mmJSON format | 1hhn.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hh/1hhn ftp://data.pdbj.org/pub/pdb/validation_reports/hh/1hhn | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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NMR ensembles |
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-Components
#1: Protein | Mass: 11907.771 Da / Num. of mol.: 1 / Fragment: P-DOMAIN RESIDUES 189-288 Source method: isolated from a genetically manipulated source Source: (gene. exp.) RATTUS NORVEGICUS (Norway rat) / Cellular location: ENDOPLASMIC RETICULUM / Plasmid: PRSET A / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): PLYSS / References: UniProt: P18418 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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-Sample preparation
Sample conditions | pH: 6.3 / Temperature: 293 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 800 MHz |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | |||||||||
NMR ensemble | Conformers submitted total number: 20 |