5HHW

Crystal structure of insulin receptor kinase domain in complex with cis-(R)-7-(3-(azetidin-1-ylmethyl)cyclobutyl)-5-(3-((tetrahydro-2H-pyran-2-yl)methoxy)phenyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine.

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 60O A 1401

Chain	Residue
A	LEU1029
A	MET1103
A	GLU1104
A	MET1106
A	ASP1110
A	ARG1163
A	MET1166
A	ASP1177
A	HOH1664
A	GLY1030
A	GLN1031
A	SER1033
A	PHE1034
A	ALA1055
A	LYS1057
A	MET1078
A	VAL1087

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site_id	AC2
Number of Residues	8
Details	binding site for residue EDO A 1402

Chain	Residue
A	ARG1020
A	ILE1023
A	LEU1025
A	PRO1129
A	PRO1130
A	HOH1634
A	HOH1670
A	HOH1694

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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	LEU1029-LYS1057

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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	ASP1183-ARG1191

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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	ASN1159

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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	SER1033
A	LYS1057
A	GLU1104
A	ARG1163
A	ASP1177

---

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

Chain	Residue	Details
A	TYR1011

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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	CYS1083

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site_id	SWS_FT_FI5
Number of Residues	2
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:26584640, ECO:0000269|PubMed:3166375, ECO:0000269|PubMed:9312016

Chain	Residue	Details
A	TYR1185
A	TYR1190

---

site_id	SWS_FT_FI6
Number of Residues	1
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	TYR1189

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site_id	SWS_FT_FI7
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:27577745

Chain	Residue	Details
A	LYS1079

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 246

Chain	Residue	Details
A	ASN1159	increase nucleophilicity, proton acceptor, proton donor, steric role
A	ARG1163	electrostatic stabiliser, increase electrophilicity, promote heterolysis
A	ASN1164	metal ligand
A	ASP1177	metal ligand

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