1B10

SOLUTION NMR STRUCTURE OF RECOMBINANT SYRIAN HAMSTER PRION PROTEIN RPRP(90-231) , 25 STRUCTURES

Replaces:  2PRP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016020	cellular_component	membrane
A	0051260	biological_process	protein homooligomerization

Functional Information from PROSITE/UniProt

site_id	PS00291
Number of Residues	16
Details	PRION_1 Prion protein signature 1. AGAAAAGAVVGGLGGY

Chain	Residue	Details
A	ALA113-TYR128

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site_id	PS00706
Number of Residues	19
Details	PRION_2 Prion protein signature 2. EtDiKIMeRVVeQMCttQY

Chain	Residue	Details
A	GLU200-TYR218

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"3138115","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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