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5JLZ

Crystal structure of HLA-DRB1*04:01 in complex with modified alpha-enolase peptide 26-40 with citrulline at the position 32

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
C0006955biological_processimmune response
C0016020cellular_componentmembrane
C0019882biological_processantigen processing and presentation
C0042613cellular_componentMHC class II protein complex
D0006955biological_processimmune response
D0016020cellular_componentmembrane
D0019882biological_processantigen processing and presentation
D0042613cellular_componentMHC class II protein complex
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue MLA D 201
ChainResidue
DGLN70
DLYS71
DALA74
DTHR77
DHOH306
FCIR32
FALA34
FVAL35

Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YDCRVEH
ChainResidueDetails
ATYR161-HIS167
BTYR171-HIS177

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:18560153
ChainResidueDetails
DASP57
DTRP61
DHIS81
DASN82
ESER40
FSER40
BHIS81
BASN82

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ESER27
FSER27
CGLY49
CALA52

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19303388, ECO:0000269|PubMed:24190431
ChainResidueDetails
DASN19
BASN19

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
CSER53

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Pathogen-derived peptide antigen => ECO:0000269|PubMed:23260142, ECO:0007744|PDB:4GBX
ChainResidueDetails
AGLU55
CGLU55

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
CASN62

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
CASN69

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
CARG76

site_idSWS_FT_FI9
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:7477400
ChainResidueDetails
AASN78
AASN118
CASN78
CASN118

220472

PDB entries from 2024-05-29

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