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6JXR

Structure of human T cell receptor-CD3 complex

Functional Information from GO Data
ChainGOidnamespacecontents
a0004888molecular_functiontransmembrane signaling receptor activity
a0007166biological_processcell surface receptor signaling pathway
a0016020cellular_componentmembrane
b0004888molecular_functiontransmembrane signaling receptor activity
b0007166biological_processcell surface receptor signaling pathway
b0016020cellular_componentmembrane
d0004888molecular_functiontransmembrane signaling receptor activity
d0007166biological_processcell surface receptor signaling pathway
d0016020cellular_componentmembrane
e0004888molecular_functiontransmembrane signaling receptor activity
e0007166biological_processcell surface receptor signaling pathway
e0016020cellular_componentmembrane
f0004888molecular_functiontransmembrane signaling receptor activity
f0007166biological_processcell surface receptor signaling pathway
f0016020cellular_componentmembrane
g0004888molecular_functiontransmembrane signaling receptor activity
g0007166biological_processcell surface receptor signaling pathway
g0016020cellular_componentmembrane
m0002250biological_processadaptive immune response
m0005886cellular_componentplasma membrane
m0009617biological_processresponse to bacterium
m0042101cellular_componentT cell receptor complex
m0042105cellular_componentalpha-beta T cell receptor complex
m0042605molecular_functionpeptide antigen binding
m0046631biological_processalpha-beta T cell activation
m0050852biological_processT cell receptor signaling pathway
n0002250biological_processadaptive immune response
n0005886cellular_componentplasma membrane
n0007166biological_processcell surface receptor signaling pathway
n0042101cellular_componentT cell receptor complex
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
nASN84
eASP23-ASP126

site_idSWS_FT_FI2
Number of Residues22
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
nTHR279-LEU301
eVAL127-SER152

site_idSWS_FT_FI3
Number of Residues10
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
nMET302-GLY312
eLYS153-ILE207

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
nASN203
mASN199

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
mASN210
mASN246
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

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PDB entries from 2024-05-01

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