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3S4S

Crystal structure of CD4 mutant bound to HLA-DR1

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
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
G0007155biological_processcell adhesion
G0016020cellular_componentmembrane
H0007155biological_processcell adhesion
H0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL B 960
ChainResidue
BARG25
BARG39

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL D 962
ChainResidue
DARG44
DVAL104
DSER133
DTYR150
EASP152

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL E 961
ChainResidue
EVAL159
EVAL129
ESER144

Functional Information from PROSITE/UniProt
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 Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:31619516, ECO:0000269|PubMed:8145819
ChainResidueDetails
BASP57
BTRP61
BHIS81
BASN82
EASP57
ETRP61
EHIS81
EASN82

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:8145819
ChainResidueDetails
BARG93
EARG93
DGLY49
DALA52

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19303388, ECO:0000269|PubMed:24190431
ChainResidueDetails
BASN19
EASN19

site_idSWS_FT_FI4
Number of Residues2
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
DSER53

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Pathogen-derived peptide antigen => ECO:0000269|PubMed:23260142, ECO:0007744|PDB:4GBX
ChainResidueDetails
AGLU55
DGLU55

site_idSWS_FT_FI6
Number of Residues2
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
DASN62

site_idSWS_FT_FI7
Number of Residues2
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
DASN69

site_idSWS_FT_FI8
Number of Residues2
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
DARG76

site_idSWS_FT_FI9
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:7477400
ChainResidueDetails
AASN78
AASN118
DASN78
DASN118

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PDB entries from 2024-11-06

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