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8QY6

Structure of interleukin 6 (gp130 P496L mutant).

Functional Information from GO Data
ChainGOidnamespacecontents
A0004896molecular_functioncytokine receptor activity
A0016020cellular_componentmembrane
B0005125molecular_functioncytokine activity
B0005138molecular_functioninterleukin-6 receptor binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0006955biological_processimmune response
B0030154biological_processcell differentiation
C0004896molecular_functioncytokine receptor activity
C0016020cellular_componentmembrane
D0004896molecular_functioncytokine receptor activity
D0016020cellular_componentmembrane
E0005125molecular_functioncytokine activity
E0005138molecular_functioninterleukin-6 receptor binding
E0005576cellular_componentextracellular region
E0005615cellular_componentextracellular space
E0006955biological_processimmune response
E0030154biological_processcell differentiation
F0004896molecular_functioncytokine receptor activity
F0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS00254
Number of Residues26
DetailsINTERLEUKIN_6 Interleukin-6 / G-CSF / MGF signature. CfqsgfneetClvkiitGLleFevyL
ChainResidueDetails
BCYS73-LEU98

site_idPS01353
Number of Residues54
DetailsHEMATOPO_REC_L_F2 Long hematopoietin receptor, gp130 family signature. NkvgkSaaavltipsphvtaaysvvnlkafpkdnllw....VeWtppPkpvsk....Yi.LeW
ChainResidueDetails
AASN402-TRP455

site_idPS01354
Number of Residues42
DetailsHEMATOPO_REC_L_F3 Long hematopoietin receptor, soluble alpha chains family signature. LqPDPPanItvtavarnprwLsvtWqdPhSWnssf..YrLrFeL
ChainResidueDetails
CLEU195-LEU236

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues690
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
CLEU1-PRO346
FLEU1-PRO346

site_idSWS_FT_FI2
Number of Residues40
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
CTHR347-LEU367
FTHR347-LEU367

site_idSWS_FT_FI3
Number of Residues162
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
CARG368-ARG449
FARG368-ARG449

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Not glycosylated => ECO:0000269|PubMed:10066782
ChainResidueDetails
CASN226
DSER837
FASN226
ASER780
ASER827
ASER837
DSER659
DSER665
DSER780
DSER827

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Cleavage; by ADAM10 and ADAM17 => ECO:0000269|PubMed:28060820
ChainResidueDetails
CPRO336
FPRO336

site_idSWS_FT_FI6
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10066782, ECO:0000269|PubMed:28060820
ChainResidueDetails
CASN36
DASN61
DASN83
DASN131
DASN157
DASN388
DASN476
DASN551
CASN74
CASN202
FASN36
FASN74
FASN202
AASN476
AASN551
DASN43

site_idSWS_FT_FI7
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:28060820
ChainResidueDetails
CASN226
CASN331
FASN226
FASN331

site_idSWS_FT_FI8
Number of Residues2
DetailsCARBOHYD: O-linked (GlcNAc) threonine => ECO:0000269|PubMed:28060820
ChainResidueDetails
CTHR333
FTHR333

223166

PDB entries from 2024-07-31

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