- PDB-1dx1: BOVINE PRION PROTEIN RESIDUES 23-230 -
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ID or keywords:
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Basic information
Entry
Database: PDB / ID: 1dx1
Title
BOVINE PRION PROTEIN RESIDUES 23-230
Components
PRION PROTEIN
Keywords
PROTEIN FIBRIL / PRION PROTEIN / REPEAT STRUCTURE
Function / homology
Function and homology information
type 5 metabotropic glutamate receptor binding / cuprous ion binding / side of membrane / inclusion body / cellular response to copper ion / molecular condensate scaffold activity / protein destabilization / protein homooligomerization / cellular response to amyloid-beta / positive regulation of peptidyl-tyrosine phosphorylation ...type 5 metabotropic glutamate receptor binding / cuprous ion binding / side of membrane / inclusion body / cellular response to copper ion / molecular condensate scaffold activity / protein destabilization / protein homooligomerization / cellular response to amyloid-beta / positive regulation of peptidyl-tyrosine phosphorylation / positive regulation of neuron apoptotic process / amyloid-beta binding / nuclear membrane / G-quadruplex RNA binding / microtubule binding / membrane raft / copper ion binding / dendrite / protein-containing complex binding / cell surface / Golgi apparatus / identical protein binding / plasma membrane / cytosol Similarity search - Function
Prion/Doppel protein, beta-ribbon domain / Major Prion Protein / Prion protein signature 1. / Prion protein signature 2. / Major prion protein N-terminal domain / Major prion protein bPrPp - N terminal / Prion protein / Major prion protein / Prion/Doppel protein, beta-ribbon domain / Prion/Doppel beta-ribbon domain superfamily ...Prion/Doppel protein, beta-ribbon domain / Major Prion Protein / Prion protein signature 1. / Prion protein signature 2. / Major prion protein N-terminal domain / Major prion protein bPrPp - N terminal / Prion protein / Major prion protein / Prion/Doppel protein, beta-ribbon domain / Prion/Doppel beta-ribbon domain superfamily / Prion/Doppel alpha-helical domain / Orthogonal Bundle / Mainly Alpha Similarity search - Domain/homology
Group: Atomic model / Derived calculations ...Atomic model / Derived calculations / Non-polymer description / Other / Structure summary / Version format compliance
Mass: 23645.928 Da / Num. of mol.: 1 / Fragment: RESIDUES 23-230 Source method: isolated from a genetically manipulated source Source: (gene. exp.) BOS TAURUS (cattle) / Cellular location: EXTRACELLULAR / Gene: PRNP / Organ: BRAIN / Plasmid: PRSET A / Cellular location (production host): CYTOPLASM / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P10279
Compound details
THE PDB ENTRIES 1DWY, 1DWZ, 1DX0 AND 1DX1 FORM A SET OF STRUCTURE DETERMINATIONS AS: 1DWY THE ...THE PDB ENTRIES 1DWY, 1DWZ, 1DX0 AND 1DX1 FORM A SET OF STRUCTURE DETERMINATIONS AS: 1DWY THE MINIMIZED CONFORMER CLOSEST TO THE MEAN OF THE FRAGMENT BPRP(121-230) (ONLY SUBMITTED RESIDUES 124-227) 1DWZ 20 MINIMIZED CONFORMERS OF THE FRAGMENT BPRP(121-230) (ONLY SUBMITTED RESIDUES 124-227) 1DX0 THE MINIMIZED CONFORMER CLOSEST TO THE MEAN OF THE FULL LENGTH BPRP(23-230) (ONLY SUBMITTED RESIDUES 124-227) 1DX1 20 MINIMIZED CONFORMERS OF THE FULL LENGTH BPRP(23-230) (ONLY SUBMITTED RESIDUES 124-227) THE SEQUENCE NUMBERING GIVEN IN THESE ENTRIES IS THAT FOR HUMAN PRION PROTEIN (RATHER THAN SEQUENTIAL) BASED ON SEQUENCE ALIGNMENT.
Sequence details
RESIDUES (GLY SER) INSERTED AT THE N-TERMINUS GLY A 21 CLONING ARTIFACT SER A 22 CLONING ARTIFACT
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Experimental details
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Experiment
Experiment
Method: SOLUTION NMR
NMR experiment
Conditions-ID
Experiment-ID
Solution-ID
Type
1
1
1
NOESY
1
2
1
COSY
NMR details
Text: CLOSEST TO THE MEAN (BACKBONE HEAVY ATOMS OF RESIDUES 125-227). THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C, 15N-LABELED PROTEIN
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