2AQ3

Crystal structure of T-cell receptor V beta domain variant complexed with superantigen SEC3

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0002250	biological_process	adaptive immune response
A	0002376	biological_process	immune system process
A	0005886	cellular_component	plasma membrane
A	0007166	biological_process	cell surface receptor signaling pathway
A	0042101	cellular_component	T cell receptor complex
B	0005576	cellular_component	extracellular region
B	0035821	biological_process	modulation of process of another organism
B	0046872	molecular_function	metal ion binding
B	0090729	molecular_function	toxin activity
C	0002250	biological_process	adaptive immune response
C	0002376	biological_process	immune system process
C	0005886	cellular_component	plasma membrane
C	0007166	biological_process	cell surface receptor signaling pathway
C	0042101	cellular_component	T cell receptor complex
D	0005576	cellular_component	extracellular region
D	0035821	biological_process	modulation of process of another organism
D	0046872	molecular_function	metal ion binding
D	0090729	molecular_function	toxin activity
E	0002250	biological_process	adaptive immune response
E	0002376	biological_process	immune system process
E	0005886	cellular_component	plasma membrane
E	0007166	biological_process	cell surface receptor signaling pathway
E	0042101	cellular_component	T cell receptor complex
F	0005576	cellular_component	extracellular region
F	0035821	biological_process	modulation of process of another organism
F	0046872	molecular_function	metal ion binding
F	0090729	molecular_function	toxin activity
G	0002250	biological_process	adaptive immune response
G	0002376	biological_process	immune system process
G	0005886	cellular_component	plasma membrane
G	0007166	biological_process	cell surface receptor signaling pathway
G	0042101	cellular_component	T cell receptor complex
H	0005576	cellular_component	extracellular region
H	0035821	biological_process	modulation of process of another organism
H	0046872	molecular_function	metal ion binding
H	0090729	molecular_function	toxin activity

Functional Information from PROSITE/UniProt

site_id	PS00277
Number of Residues	10
Details	STAPH_STREP_TOXIN_1 Staphylococcal enterotoxin/Streptococcal pyrogenic exotoxin signature 1. YGGITKHegN

Chain	Residue	Details
B	TYR110-ASN119

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site_id	PS00278
Number of Residues	24
Details	STAPH_STREP_TOXIN_2 Staphyloccocal enterotoxin/Streptococcal pyrogenic exotoxin signature 2. KksVtaqeLDikaRnfLinkknLY

Chain	Residue	Details
B	LYS149-TYR172

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20836565","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2008","submissionDatabase":"PDB data bank","title":"Manipulating the coupled folding and binding process drives affinity maturation in a protein-protein complex.","authors":["Cho S.","Swaminathan C.P.","Kerzic M.C.","Guan R.","Yang J.","Kieke M.C.","Andersen P.S.","Krantz D.M.","Mariuzza R.A.","Eric S.J."]}},{"source":"PDB","id":"3BVG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3BVM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3BVZ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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