7SL2
Full-length insulin receptor bound with site 2 binding deficient mutant insulin (A-L13R) -- asymmetric conformation
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein kinase activity |
A | 0004713 | molecular_function | protein tyrosine kinase activity |
A | 0004714 | molecular_function | transmembrane receptor protein tyrosine kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006468 | biological_process | protein phosphorylation |
A | 0007169 | biological_process | cell surface receptor protein tyrosine kinase signaling pathway |
A | 0016020 | cellular_component | membrane |
A | 0043548 | molecular_function | phosphatidylinositol 3-kinase binding |
A | 0043560 | molecular_function | insulin receptor substrate binding |
A | 0046777 | biological_process | protein autophosphorylation |
B | 0004672 | molecular_function | protein kinase activity |
B | 0004713 | molecular_function | protein tyrosine kinase activity |
B | 0004714 | molecular_function | transmembrane receptor protein tyrosine kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0006468 | biological_process | protein phosphorylation |
B | 0007169 | biological_process | cell surface receptor protein tyrosine kinase signaling pathway |
B | 0016020 | cellular_component | membrane |
B | 0043548 | molecular_function | phosphatidylinositol 3-kinase binding |
B | 0043560 | molecular_function | insulin receptor substrate binding |
B | 0046777 | biological_process | protein autophosphorylation |
C | 0005179 | molecular_function | hormone activity |
C | 0005576 | cellular_component | extracellular region |
D | 0005179 | molecular_function | hormone activity |
D | 0005576 | cellular_component | extracellular region |
E | 0005179 | molecular_function | hormone activity |
E | 0005576 | cellular_component | extracellular region |
F | 0005179 | molecular_function | hormone activity |
F | 0005576 | cellular_component | extracellular region |
G | 0005179 | molecular_function | hormone activity |
G | 0005576 | cellular_component | extracellular region |
H | 0005179 | molecular_function | hormone activity |
H | 0005576 | cellular_component | extracellular region |
I | 0005179 | molecular_function | hormone activity |
I | 0005576 | cellular_component | extracellular region |
J | 0005179 | molecular_function | hormone activity |
J | 0005576 | cellular_component | extracellular region |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 29 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGQGSFGMVYeGnakdiikgeaetr.....VAVK |
Chain | Residue | Details |
A | LEU992-LYS1020 |
site_id | PS00109 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLAARNCMV |
Chain | Residue | Details |
A | PHE1118-VAL1130 |
site_id | PS00239 |
Number of Residues | 9 |
Details | RECEPTOR_TYR_KIN_II Receptor tyrosine kinase class II signature. DIYetdYYR |
Chain | Residue | Details |
A | ASP1146-ARG1154 |
site_id | PS00262 |
Number of Residues | 15 |
Details | INSULIN Insulin family signature. CCTSiCSryqLenyC |
Chain | Residue | Details |
G | CYS6-CYS20 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 16 |
Details | Region: {"description":"Insulin-binding","evidences":[{"evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | Site: {"description":"Insulin-binding","evidences":[{"evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P06213","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P06213","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 28 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19656770","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 80 |
Details | Peptide: {"description":"Insulin A chain","featureId":"PRO_0000015821"} |
Chain | Residue | Details |