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2XN9

Crystal structure of the ternary complex between human T cell receptor, staphylococcal enterotoxin H and human major histocompatibility complex class II

Functional Information from GO Data
ChainGOidnamespacecontents
C0005576cellular_componentextracellular region
C0035821biological_processmodulation of process of another organism
C0042289molecular_functionMHC class II protein binding
C0042608molecular_functionT cell receptor binding
C0046872molecular_functionmetal ion binding
C0090729molecular_functiontoxin activity
D0006955biological_processimmune response
D0016020cellular_componentmembrane
D0019882biological_processantigen processing and presentation
D0042613cellular_componentMHC class II protein complex
E0006955biological_processimmune response
E0016020cellular_componentmembrane
E0019882biological_processantigen processing and presentation
E0042613cellular_componentMHC class II protein complex
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA C 1216
ChainResidue
AHOH2030
CHIS23
CSER77
CHOH2011
CHOH2028

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 1201
ChainResidue
BSER168
BARG195
BGOL1245
AGLU17
AARG163
ASER164
AHOH2092

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 1245
ChainResidue
AGLU17
AGOL1201
AHOH2092
BVAL196
BSER197

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 1246
ChainResidue
BARG110
BASP153
BGLN175
BPRO176
BTYR188

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 1247
ChainResidue
BASN30
BHIS31
BASP32
BSER97
BARG98

Functional Information from PROSITE/UniProt
site_idPS00278
Number of Residues24
DetailsSTAPH_STREP_TOXIN_2 Staphyloccocal enterotoxin/Streptococcal pyrogenic exotoxin signature 2. KknVtlqeLDikiRkiLsdkykIY
ChainResidueDetails
CLYS130-TYR153

site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YDCRVEH
ChainResidueDetails
DTYR161-HIS167
ETYR171-HIS177

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:31619516, ECO:0000269|PubMed:8145819
ChainResidueDetails
EASP57
ETRP61
EHIS81
EASN82

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:8145819
ChainResidueDetails
EARG93
DALA52

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19303388, ECO:0000269|PubMed:24190431
ChainResidueDetails
EASN19

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Self- and pathogen-derived peptide antigen => ECO:0000269|PubMed:17583734, ECO:0000269|PubMed:21115828, ECO:0000269|PubMed:31619516, ECO:0000269|PubMed:8145819
ChainResidueDetails
DSER53

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Pathogen-derived peptide antigen => ECO:0000269|PubMed:23260142, ECO:0007744|PDB:4GBX
ChainResidueDetails
DGLU55

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Self- and pathogen-derived peptide antigen => ECO:0000269|PubMed:17583734, ECO:0000269|PubMed:21115828, ECO:0000269|PubMed:23260142, ECO:0000269|PubMed:31619516, ECO:0000269|PubMed:8145819, ECO:0007744|PDB:4GBX
ChainResidueDetails
DASN62

site_idSWS_FT_FI7
Number of Residues1
DetailsSITE: Pathogen-derived peptide antigen => ECO:0000269|PubMed:17583734, ECO:0000269|PubMed:21115828, ECO:0000269|PubMed:23260142, ECO:0000269|PubMed:8145819, ECO:0007744|PDB:4FQX, ECO:0007744|PDB:4GBX
ChainResidueDetails
DASN69

site_idSWS_FT_FI8
Number of Residues1
DetailsSITE: Self- and pathogen-derived peptide antigen => ECO:0000269|PubMed:17583734, ECO:0000269|PubMed:23260142, ECO:0000269|PubMed:31619516, ECO:0000269|PubMed:8145819, ECO:0007744|PDB:4FQX, ECO:0007744|PDB:4GBX
ChainResidueDetails
DARG76

site_idSWS_FT_FI9
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:7477400
ChainResidueDetails
DASN78
DASN118

219140

PDB entries from 2024-05-01

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