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6UJ8

Crystal structure of HLA-B*07:02 with wild-type IDH2 peptide

Functional Information from GO Data
ChainGOidnamespacecontents
B0006955biological_processimmune response
B0042612cellular_componentMHC class I protein complex
E0006955biological_processimmune response
E0042612cellular_componentMHC class I protein complex
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue PEG A 301
ChainResidue
AASP29
AASP30
A1PE302
BTYR83

site_idAC2
Number of Residues7
Detailsbinding site for residue 1PE A 302
ChainResidue
BSER72
BTYR83
ATYR27
AARG48
APRO235
APHE241
APEG301

site_idAC3
Number of Residues6
Detailsbinding site for residue PEG A 303
ChainResidue
AGLU163
AGLU166
ATRP167
AHOH419
AHOH450
DGLU154

site_idAC4
Number of Residues3
Detailsbinding site for residue SO4 A 304
ChainResidue
AGLU232
ATHR233
ALYS243

site_idAC5
Number of Residues2
Detailsbinding site for residue PEG B 201
ChainResidue
BSER77
BLYS78

site_idAC6
Number of Residues6
Detailsbinding site for residue PGE B 202
ChainResidue
APHE8
AMET98
AGLN115
BPHE76
BSER77
BLYS78

site_idAC7
Number of Residues2
Detailsbinding site for residue PEG B 203
ChainResidue
BILE27
BLYS111

site_idAC8
Number of Residues7
Detailsbinding site for residue PG4 D 301
ChainResidue
DTYR27
DASP29
DASP30
DTHR233
DPHE241
DPEG302
EHOH318

site_idAC9
Number of Residues3
Detailsbinding site for residue PEG D 302
ChainResidue
DPG4301
DSO4303
DHOH447

site_idAD1
Number of Residues2
Detailsbinding site for residue SO4 D 303
ChainResidue
DPEG302
DHOH414

site_idAD2
Number of Residues2
Detailsbinding site for residue PEG E 201
ChainResidue
EPRO25
ELYS111

Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACRVNH
ChainResidueDetails
BTYR98-HIS104
ATYR257-HIS263

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues348
DetailsDomain: {"description":"Ig-like C1-type"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues182
DetailsRegion: {"description":"Alpha-2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues182
DetailsRegion: {"description":"Alpha-3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues12
DetailsMotif: {"description":"Bw6 motif","evidences":[{"source":"PubMed","id":"25480565","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25808313","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Pyrrolidone carboxylic acid; in form pI 5.3","evidences":[{"source":"PubMed","id":"7554280","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (Glc) (glycation) isoleucine; in hemodialysis-associated amyloidosis","evidences":[{"source":"PubMed","id":"7918443","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues12
DetailsGlycosylation: {"description":"N-linked (Glc) (glycation) lysine; in vitro","evidences":[{"source":"PubMed","id":"7918443","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P33198","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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