7STH

Full-length insulin receptor bound with unsaturated insulin WT (2 insulin bound) symmetric 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

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	LEU991-LYS1019

---

site_id	PS00109
Number of Residues	13
Details	PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLAARNCMV

Chain	Residue	Details
A	PHE1117-VAL1129

---

site_id	PS00239
Number of Residues	9
Details	RECEPTOR_TYR_KIN_II Receptor tyrosine kinase class II signature. DIYetdYYR

Chain	Residue	Details
A	ASP1145-ARG1153

---

site_id	PS00262
Number of Residues	15
Details	INSULIN Insulin family signature. CCTSiCSlyqLenyC

Chain	Residue	Details
C	CYS61-CYS75

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1826
Details	TOPO_DOM: Extracellular => ECO:0000305

Chain	Residue	Details
A	HIS1-SER720
A	SER725-LYS918
B	HIS1-SER720
B	SER725-LYS918

---

site_id	SWS_FT_FI2
Number of Residues	40
Details	TRANSMEM: Helical => ECO:0000255

Chain	Residue	Details
A	ILE919-LEU939
B	ILE919-LEU939

---

site_id	SWS_FT_FI3
Number of Residues	808
Details	TOPO_DOM: Cytoplasmic => ECO:0000305

Chain	Residue	Details
A	PHE940-SER1344
B	PHE940-SER1344

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	ACT_SITE: Proton donor/acceptor => ECO:0000250

Chain	Residue	Details
A	ASP1121
B	ASP1121

---

site_id	SWS_FT_FI5
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	SER995
A	GLU1066
A	ARG1125
A	ASP1139
B	SER995
B	GLU1066
B	ARG1125
B	ASP1139

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	BINDING:

Chain	Residue	Details
A	LYS1019
B	LYS1019

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	SITE: Insulin-binding => ECO:0000250

Chain	Residue	Details
A	PHE39
B	PHE39

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P06213

Chain	Residue	Details
A	SER373
A	SER380
B	SER373
B	SER380

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P06213

Chain	Residue	Details
A	TYR374
B	TYR374

---

site_id	SWS_FT_FI10
Number of Residues	8
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000250|UniProtKB:P06213

Chain	Residue	Details
A	TYR961
A	TYR1147
A	TYR1317
A	TYR1323
B	TYR961
B	TYR1147
B	TYR1317
B	TYR1323

---

site_id	SWS_FT_FI11
Number of Residues	2
Details	MOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:P06213

Chain	Residue	Details
A	CYS1045
B	CYS1045

---

site_id	SWS_FT_FI12
Number of Residues	4
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:20655470

Chain	Residue	Details
A	TYR1151
A	TYR1152
B	TYR1151
B	TYR1152

---

site_id	SWS_FT_FI13
Number of Residues	34
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN16
A	ASN514
A	ASN606
A	ASN624
A	ASN672
A	ASN731
A	ASN744
A	ASN882
A	ASN895
B	ASN16
B	ASN25
A	ASN25
B	ASN78
B	ASN111
B	ASN215
B	ASN255
B	ASN295
B	ASN337
B	ASN397
B	ASN514
B	ASN606
B	ASN624
A	ASN78
B	ASN672
B	ASN731
B	ASN744
B	ASN882
B	ASN895
A	ASN111
A	ASN215
A	ASN255
A	ASN295
A	ASN337
A	ASN397

---

site_id	SWS_FT_FI14
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:19656770

Chain	Residue	Details
A	ASN418
B	ASN418

---