3EKN

Insulin receptor kinase complexed with an inhibitor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein 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

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE GS3 A 1

Chain	Residue
A	ARG1000
A	GLY1082
A	SER1086
A	MET1139
A	HOH1341
A	HOH1345
A	HOH1388
A	HOH1389
A	HOH1497
A	LEU1002
A	GLN1004
A	GLY1005
A	ALA1028
A	VAL1060
A	MET1076
A	GLU1077
A	MET1079

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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

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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

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:9312016

Chain	Residue	Details
A	ASN1132

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site_id	SWS_FT_FI2
Number of Residues	5
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:18278056

Chain	Residue	Details
A	SER1006
A	LYS1030
A	GLU1077
A	ARG1136
A	ASP1150

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000305

Chain	Residue	Details
A	TYR984

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:38056462

Chain	Residue	Details
A	CYS1056

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site_id	SWS_FT_FI5
Number of Residues	3
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:14690593, ECO:0000269|PubMed:16246733, ECO:0000269|PubMed:16271887, ECO:0000269|PubMed:18278056, ECO:0000269|PubMed:18767165, ECO:0000269|PubMed:3166375, ECO:0000269|PubMed:9312016

Chain	Residue	Details
A	TYR1158
A	TYR1162
A	TYR1163

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Catalytic Information from CSA

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

Chain	Residue	Details
A	ASN1132
A	ARG1136

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site_id	MCSA1
Number of Residues	4
Details	M-CSA 246

Chain	Residue	Details
A	ASN1132	increase nucleophilicity, proton acceptor, proton donor, steric role
A	ARG1136	electrostatic stabiliser, increase electrophilicity, promote heterolysis
A	ASN1137	metal ligand
A	ASP1150	metal ligand

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