3ETA

Kinase domain of insulin receptor complexed with a pyrrolo pyridine inhibitor

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
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

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE 351 A2001

Chain	Residue
A	LEU1002
A	PHE1128
A	MET1139
A	ILE1148
A	GLY1149
A	ASP1150
A	HOH3155
A	ALA1028
A	LYS1030
A	GLU1047
A	MET1051
A	VAL1059
A	VAL1060
A	GLU1077
A	MET1079

---

site_id	AC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE 351 B2001

Chain	Residue
B	LEU1002
B	ALA1028
B	GLU1047
B	VAL1050
B	MET1051
B	VAL1060
B	MET1076
B	GLU1077
B	MET1079
B	GLY1082
B	PHE1128
B	MET1139
B	ILE1148
B	GLY1149
B	ASP1150

---

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	29
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGQGSFGMVYeGnardiikgeaetr.....VAVK

Chain	Residue	Details
A	LEU1002-LYS1030

---

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

Chain	Residue	Details
A	PHE1128-VAL1140

---

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

Chain	Residue	Details
A	ASP1156-ARG1164

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"9312016","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18278056","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Modified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"PubMed","id":"38056462","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"14690593","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16246733","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16271887","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18278056","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18767165","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26584640","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3166375","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9312016","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"14690593","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16246733","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16271887","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18278056","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18767165","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3166375","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9312016","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"27577745","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ASP1132
A	ARG1136

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
B	ASP1132
B	ARG1136

---

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ASP1132
A	ALA1134

---

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
B	ASP1132
B	ALA1134

---

site_id	CSA5
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ASP1132
A	ASN1137
A	ALA1134

---

site_id	CSA6
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
B	ASP1132
B	ASN1137
B	ALA1134

---

site_id	MCSA1
Number of Residues	4
Details	M-CSA 246

Chain	Residue	Details
A	ASP1132	increase nucleophilicity, proton acceptor, proton donor, steric role
A	ARG1136	electrostatic stabiliser, increase electrophilicity, promote heterolysis
A	ASN1137	metal ligand
A	ASP1150	metal ligand

---

site_id	MCSA2
Number of Residues	4
Details	M-CSA 246

Chain	Residue	Details
B	ASP1132	increase nucleophilicity, proton acceptor, proton donor, steric role
B	ARG1136	electrostatic stabiliser, increase electrophilicity, promote heterolysis
B	ASN1137	metal ligand
B	ASP1150	metal ligand

---