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8ZA6

Cryo-EM structure of the gdTCR-CD3 complex

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues93
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
gGLN23-SER116
fASP23-ASP126

site_idSWS_FT_FI2
Number of Residues20
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
gGLY117-ALA137
fVAL127-SER152

site_idSWS_FT_FI3
Number of Residues44
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
gGLY138-ASN182
fLYS153-ILE207

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:2540970, ECO:0000269|PubMed:3112151
ChainResidueDetails
gSER145
fTYR188

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKC => ECO:0000269|PubMed:2540970, ECO:0000269|PubMed:3112151, ECO:0000269|PubMed:8187769
ChainResidueDetails
gSER148
fTYR199
bTYR64
bTYR72

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:8636209
ChainResidueDetails
gASN52
gASN92

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:12522270, ECO:0007744|PubMed:15144186, ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:19690332
ChainResidueDetails
aTYR111
aTYR142
bTYR111
bTYR142

site_idSWS_FT_FI8
Number of Residues4
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19690332
ChainResidueDetails
aTYR123
aTYR153
bTYR123
bTYR153

237423

PDB entries from 2025-06-11

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