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1HXY

CRYSTAL STRUCTURE OF STAPHYLOCOCCAL ENTEROTOXIN H IN COMPLEX WITH HUMAN MHC CLASS II

Functional Information from GO Data
ChainGOidnamespacecontents
A0006955biological_processimmune response
A0016020cellular_componentmembrane
A0019882biological_processantigen processing and presentation
A0042613cellular_componentMHC class II protein complex
B0006955biological_processimmune response
B0016020cellular_componentmembrane
B0019882biological_processantigen processing and presentation
B0042613cellular_componentMHC class II protein complex
D0005576cellular_componentextracellular region
D0035821biological_processmodulation of process of another organism
D0042289molecular_functionMHC class II protein binding
D0042608molecular_functionT cell receptor binding
D0046872molecular_functionmetal ion binding
D0090729molecular_functiontoxin activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN D 600
ChainResidue
BHIS81
DHIS206
DASP208

Functional Information from PROSITE/UniProt
site_idPS00278
Number of Residues24
DetailsSTAPH_STREP_TOXIN_2 Staphyloccocal enterotoxin/Streptococcal pyrogenic exotoxin signature 2. KknVtlqeLDikiRkiLsdkykIY
ChainResidueDetails
DLYS130-TYR153

site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCQVEH
ChainResidueDetails
BTYR171-HIS177
ATYR161-HIS167

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:10986116
ChainResidueDetails
DASP167
BTRP61
BHIS81
BASN82

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10986116, ECO:0000269|PubMed:11432818, ECO:0007744|PDB:1EWC, ECO:0007744|PDB:1HXY
ChainResidueDetails
DHIS206
AALA52

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:11432818, ECO:0007744|PDB:1EWC, ECO:0007744|PDB:1HXY
ChainResidueDetails
DASP208

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
ASER53

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Pathogen-derived peptide antigen => ECO:0000269|PubMed:23260142, ECO:0007744|PDB:4GBX
ChainResidueDetails
AGLU55

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
AASN62

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
AASN69

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
AARG76

site_idSWS_FT_FI9
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:7477400
ChainResidueDetails
AASN78
AASN118

222415

PDB entries from 2024-07-10

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