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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2RF9

Crystal structure of the complex between the EGFR kinase domain and a Mig6 peptide

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	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

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
A	LEU694-LYS721

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

Chain	Residue	Details
A	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
A	ASP813
B	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
A	LEU694
B	LEU694

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
A	LYS721
B	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
A	THR766
B	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
A	ASP831
B	ASP831

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

Chain	Residue	Details
A	TYR992
B	TYR992

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269\|PubMed:29192674

Chain	Residue	Details
A	LYS721
B	LYS721

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0000269\|PubMed:23774213

Chain	Residue	Details
A	TYR845
B	TYR845

site_id	SWS_FT_FI9
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
A	SER967
B	SER967

site_id	SWS_FT_FI10
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18669648

Chain	Residue	Details
A	SER971
B	SER971

site_id	SWS_FT_FI11
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269\|PubMed:19563760, ECO:0007744\|PubMed:18669648

Chain	Residue	Details
A	TYR974
B	TYR974

site_id	SWS_FT_FI12
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269\|PubMed:19563760, ECO:0000269\|PubMed:23774213

Chain	Residue	Details
A	TYR992
B	TYR992

site_id	SWS_FT_FI13
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
A	LYS692
A	LYS713
A	LYS730
A	LYS843
B	LYS692
B	LYS713
B	LYS730
B	LYS843

site_id	SWS_FT_FI14
Number of Residues	6
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269\|PubMed:16543144

Chain	Residue	Details
A	LYS905
A	LYS946
B	LYS905
B	LYS946

site_id	SWS_FT_FI15
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269\|PubMed:33996800

Chain	Residue	Details
A	LYS733
A	LYS936
B	LYS733
B	LYS936

Catalytic Information from CSA

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

Chain	Residue	Details
A	ARG817
A	ASP813

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

Chain	Residue	Details
B	ARG817
B	ASP813

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

Chain	Residue	Details
A	ASP813
A	ALA815

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

Chain	Residue	Details
B	ASP813
B	ALA815

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

Chain	Residue	Details
A	ASP813
A	ASN818
A	ALA815

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

Chain	Residue	Details
B	ASP813
B	ASN818
B	ALA815

227344

PDB entries from 2024-11-13

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