6DU9

Crystal Structure of Human Prion Protein 90-231

Functional Information from GO Data

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue CD A 301

Chain	Residue
A	HIS177
A	HIS177
A	CL304
A	CL304

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site_id	AC2
Number of Residues	5
Details	binding site for residue CD A 302

Chain	Residue
A	HIS140
A	ASP147
A	HOH402
A	HOH404
A	HOH411

---

site_id	AC3
Number of Residues	4
Details	binding site for residue CD A 303

Chain	Residue
A	ASP178
A	GLU207
A	HOH416
A	HOH417

---

site_id	AC4
Number of Residues	4
Details	binding site for residue CL A 304

Chain	Residue
A	HIS177
A	HIS177
A	CD301
A	CD301

---

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

---

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

Chain	Residue	Details
A	GLU200-TYR218

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12214108","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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