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6O9B

Crystal structure of HLA-A3*01 in complex with a wild-type beta-catenin peptide

Functional Information from GO Data
ChainGOidnamespacecontents
B0006955biological_processimmune response
B0042612cellular_componentMHC class I protein complex
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue PG4 A 301
ChainResidue
AARG21
BSER53
BASP54

site_idAC2
Number of Residues11
Detailsbinding site for residue MES A 302
ChainResidue
AARG273
ATRP274
AGLU275
AHOH404
AHOH421
AASN127
AASP129
AARG131
ASER132
AHIS188
AMET189

site_idAC3
Number of Residues6
Detailsbinding site for residue IMD A 303
ChainResidue
ASER2
AHIS3
AASP29
AARG181
ATHR182
AGLU264

site_idAC4
Number of Residues1
Detailsbinding site for residue IMD A 304
ChainResidue
AGLU166

site_idAC5
Number of Residues5
Detailsbinding site for residue PEG A 305
ChainResidue
AARG6
ATYR27
AASP29
AASP30
BMES202

site_idAC6
Number of Residues3
Detailsbinding site for residue PEG A 306
ChainResidue
AMET45
AGLU53
ATRP60

site_idAC7
Number of Residues1
Detailsbinding site for residue EDO A 307
ChainResidue
ASER4

site_idAC8
Number of Residues4
Detailsbinding site for residue EDO A 308
ChainResidue
AHIS192
ATHR200
AARG202
AHOH457

site_idAC9
Number of Residues1
Detailsbinding site for residue EDO A 309
ChainResidue
AGLY16

site_idAD1
Number of Residues1
Detailsbinding site for residue EDO A 310
ChainResidue
ATYR84

site_idAD2
Number of Residues7
Detailsbinding site for residue PG4 B 201
ChainResidue
APHE8
AMET98
AARG111
AGLN115
BSER77
BLYS78
BMES202

site_idAD3
Number of Residues9
Detailsbinding site for residue MES B 202
ChainResidue
AALA211
APHE241
APEG305
BTYR46
BSER77
BLYS78
BTYR83
BPG4201
BMES203

site_idAD4
Number of Residues7
Detailsbinding site for residue MES B 203
ChainResidue
AGLU232
ATHR233
ALYS243
AHOH476
BSER77
BASP79
BMES202

site_idAD5
Number of Residues7
Detailsbinding site for residue PEG B 204
ChainResidue
AHIS188
ATRP204
AGLN242
BSER31
BARG32
BHIS33
BPRO34

site_idAD6
Number of Residues2
Detailsbinding site for residue PEG B 205
ChainResidue
BASN103
BHIS104

site_idAD7
Number of Residues4
Detailsbinding site for residue EDO B 206
ChainResidue
BGLU56
BASP58
BARG101
BASN103

site_idAD8
Number of Residues1
Detailsbinding site for residue EDO B 207
ChainResidue
BLYS111

site_idAD9
Number of Residues1
Detailsbinding site for residue EDO B 208
ChainResidue
BSER108

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues86
DetailsDomain: {"description":"Ig-like C1-type","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues89
DetailsRegion: {"description":"Alpha-1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues91
DetailsRegion: {"description":"Alpha-2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues91
DetailsRegion: {"description":"Alpha-3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21943705","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21543847","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Sulfotyrosine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues88
DetailsDomain: {"description":"Ig-like C1-type"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Pyrrolidone carboxylic acid; in form pI 5.3","evidences":[{"source":"PubMed","id":"7554280","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (Glc) (glycation) isoleucine; in hemodialysis-associated amyloidosis","evidences":[{"source":"PubMed","id":"7918443","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues6
DetailsGlycosylation: {"description":"N-linked (Glc) (glycation) lysine; in vitro","evidences":[{"source":"PubMed","id":"7918443","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by GSK3-beta","evidences":[{"source":"PubMed","id":"12027456","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30714168","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"12051714","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"24824780","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

250059

PDB entries from 2026-03-04

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