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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4RIY

Crystal structure of an EGFR/HER3 kinase domain heterodimer containing the cancer-associated HER3-E909G mutation

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
B	0004672	molecular_function	protein kinase activity
B	0004713	molecular_function	protein tyrosine kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation
C	0004672	molecular_function	protein kinase activity
C	0005524	molecular_function	ATP binding
C	0006468	biological_process	protein phosphorylation
D	0004672	molecular_function	protein kinase activity
D	0004713	molecular_function	protein tyrosine kinase activity
D	0005524	molecular_function	ATP binding
D	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE ANP A 1101

Chain	Residue
A	GLY697
A	ASN815
A	ARG819
A	ASN820
A	LEU822
A	ASP833
A	MG1102
A	SER698
A	GLY699
A	VAL700
A	VAL704
A	CYS721
A	LYS723
A	GLN769
A	LEU771

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 1102

Chain	Residue
A	ASN820
A	ASP833
A	ANP1101

site_id	AC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE ADP B 1001

Chain	Residue
B	PHE699
B	VAL702
B	ALA719
B	LYS721
B	THR766
B	GLN767
B	LEU768
B	MET769
B	CYS773
B	ASN818
B	LEU820
B	ASP831
B	MG1002

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG B 1002

Chain	Residue
B	ASN818
B	ADP1001

site_id	AC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE ANP C 1101

Chain	Residue
C	GLY697
C	SER698
C	GLY699
C	VAL700
C	VAL704
C	LYS723
C	GLN769
C	LEU771
C	ASN815
C	ARG819
C	ASN820
C	LEU822
C	ASP833
C	MG1102

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG C 1102

Chain	Residue
C	ASN820
C	ASP833
C	ANP1101

site_id	AC7
Number of Residues	14
Details	BINDING SITE FOR RESIDUE ADP D 1001

Chain	Residue
D	LEU694
D	PHE699
D	VAL702
D	ALA719
D	LYS721
D	THR766
D	GLN767
D	LEU768
D	MET769
D	ARG817
D	ASN818
D	LEU820
D	ASP831
D	MG1002

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG D 1002

Chain	Residue
D	ASN818
D	ADP1001

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	28
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGAFGTVYkGlwipegekvkip......VAIK

Chain	Residue	Details
B	LEU694-LYS721

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

Chain	Residue	Details
B	LEU809-VAL821

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000255\|PROSITE-ProRule:PRU00159, ECO:0000255\|PROSITE-ProRule:PRU10028

Chain	Residue	Details
B	ASP813
D	ASP813

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:19563760, ECO:0007744\|PDB:2GS7, ECO:0007744\|PDB:3GT8, ECO:0007744\|PDB:4ZSE, ECO:0007744\|PDB:5CNN, ECO:0007744\|PDB:5CNO, ECO:0007744\|PDB:5D41

Chain	Residue	Details
B	LEU694
D	LEU694
A	GLN769
A	ASN815
C	LEU696
C	LYS723
C	GLN769
C	ASN815

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:17349580, ECO:0000269\|PubMed:19563760, ECO:0007744\|PDB:2EB3, ECO:0007744\|PDB:2GS7, ECO:0007744\|PDB:2ITN, ECO:0007744\|PDB:3GT8, ECO:0007744\|PDB:3VJN, ECO:0007744\|PDB:3VJO, ECO:0007744\|PDB:4RIW, ECO:0007744\|PDB:4RIY, ECO:0007744\|PDB:4ZSE, ECO:0007744\|PDB:5CNN, ECO:0007744\|PDB:5CNO, ECO:0007744\|PDB:5D41

Chain	Residue	Details
B	LYS721
D	LYS721

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:17349580, ECO:0000269\|PubMed:19563760, ECO:0007744\|PDB:2EB3, ECO:0007744\|PDB:2GS7, ECO:0007744\|PDB:2ITN, ECO:0007744\|PDB:2ITV, ECO:0007744\|PDB:2ITX, ECO:0007744\|PDB:3GT8, ECO:0007744\|PDB:3VJN, ECO:0007744\|PDB:3VJO, ECO:0007744\|PDB:4RIW, ECO:0007744\|PDB:4RIX, ECO:0007744\|PDB:4RIY, ECO:0007744\|PDB:4ZSE, ECO:0007744\|PDB:5CNN, ECO:0007744\|PDB:5CNO, ECO:0007744\|PDB:5D41

Chain	Residue	Details
B	THR766
D	THR766

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:17349580, ECO:0000269\|PubMed:19563760, ECO:0007744\|PDB:2EB3, ECO:0007744\|PDB:2GS7, ECO:0007744\|PDB:2ITN, ECO:0007744\|PDB:2ITV, ECO:0007744\|PDB:2ITX, ECO:0007744\|PDB:3GT8, ECO:0007744\|PDB:3VJN, ECO:0007744\|PDB:4RIW, ECO:0007744\|PDB:4RIX, ECO:0007744\|PDB:4RIY, ECO:0007744\|PDB:4ZSE, ECO:0007744\|PDB:5CNN, ECO:0007744\|PDB:5CNO, ECO:0007744\|PDB:5D41

Chain	Residue	Details
B	ASP831
D	ASP831

site_id	SWS_FT_FI6
Number of Residues	2
Details	SITE: Important for interaction with PIK3C2B

Chain	Residue	Details
B	TYR992
D	TYR992

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by PKD/PRKD1 => ECO:0000269\|PubMed:10523301, ECO:0000269\|PubMed:16083266, ECO:0000269\|PubMed:3138233, ECO:0007744\|PubMed:18691976, ECO:0007744\|PubMed:20068231, ECO:0007744\|PubMed:23186163, ECO:0007744\|PubMed:24275569

Chain	Residue	Details
B	THR669
D	THR669

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000269\|PubMed:3138233, ECO:0007744\|PubMed:18691976

Chain	Residue	Details
B	SER671
D	SER671

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269\|PubMed:29192674

Chain	Residue	Details
B	LYS721
D	LYS721

site_id	SWS_FT_FI10
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0000269\|PubMed:23774213

Chain	Residue	Details
B	TYR845
D	TYR845

site_id	SWS_FT_FI11
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000269\|PubMed:16083266, ECO:0007744\|PubMed:18669648, ECO:0007744\|PubMed:20068231, ECO:0007744\|PubMed:24275569

Chain	Residue	Details
B	SER967
D	SER967

site_id	SWS_FT_FI12
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18669648

Chain	Residue	Details
B	SER971
D	SER971

site_id	SWS_FT_FI13
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269\|PubMed:19563760, ECO:0007744\|PubMed:18669648

Chain	Residue	Details
B	TYR974
D	TYR974

site_id	SWS_FT_FI14
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269\|PubMed:19563760, ECO:0000269\|PubMed:23774213

Chain	Residue	Details
B	TYR992
D	TYR992

site_id	SWS_FT_FI15
Number of Residues	8
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269\|PubMed:16543144, ECO:0000269\|PubMed:33996800

Chain	Residue	Details
B	LYS692
B	LYS713
B	LYS730
B	LYS843
D	LYS692
D	LYS713
D	LYS730
D	LYS843

site_id	SWS_FT_FI16
Number of Residues	6
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269\|PubMed:16543144

Chain	Residue	Details
B	LYS905
B	LYS946
D	LYS905
D	LYS946

site_id	SWS_FT_FI17
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269\|PubMed:33996800

Chain	Residue	Details
B	LYS733
B	LYS936
D	LYS733
D	LYS936

218853

PDB entries from 2024-04-24

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