2AQ2
Crystal structure of T-cell receptor V beta domain variant complexed with superantigen SEC3 mutant
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN B 1001 |
Chain | Residue |
B | ASP83 |
B | HIS116 |
B | HIS120 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NA B 1002 |
Chain | Residue |
A | GLU1 |
B | PHE174 |
B | ASN175 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE NA B 1003 |
Chain | Residue |
B | LYS25 |
B | PHE174 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA B 1004 |
Chain | Residue |
B | THR114 |
B | LYS115 |
B | HOH1150 |
B | TYR77 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 500 |
Chain | Residue |
A | TYR33 |
A | HOH174 |
B | HIS47 |
B | ASN70 |
B | GLU71 |
site_id | AC6 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SO4 B 501 |
Chain | Residue |
A | HOH131 |
B | TYR26 |
B | HIS31 |
B | ASP55 |
B | ASN60 |
B | ASN88 |
B | TYR90 |
B | HOH1050 |
B | HOH1086 |
B | HOH1088 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 502 |
Chain | Residue |
B | LYS75 |
B | ARG138 |
B | HOH1038 |
B | HOH1142 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 503 |
Chain | Residue |
B | LYS75 |
B | LYS78 |
B | ARG138 |
B | HOH1059 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 504 |
Chain | Residue |
B | GLY203 |
B | ASP204 |
B | LYS205 |
B | HOH1151 |
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 |
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 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
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 |