Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6P1L

Crystal structure of EGFR in complex with EAI045

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
C	0004672	molecular_function	protein kinase activity
C	0004713	molecular_function	protein tyrosine 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	4
Details	binding site for residue MG A 1101

Chain	Residue
A	ASN842
A	ASP855
A	ANP1102
A	HOH1202

site_id	AC2
Number of Residues	19
Details	binding site for residue ANP A 1102

Chain	Residue
A	VAL726
A	ALA743
A	LYS745
A	MET790
A	GLN791
A	MET793
A	ASP837
A	ARG841
A	ASN842
A	LEU844
A	ASP855
A	MG1101
A	9LL1103
A	HOH1202
A	LEU718
A	SER720
A	GLY721
A	ALA722
A	GLY724

site_id	AC3
Number of Residues	15
Details	binding site for residue 9LL A 1103

Chain	Residue
A	VAL726
A	ALA743
A	LYS745
A	ILE759
A	ALA763
A	MET766
A	CYS775
A	ARG776
A	LEU777
A	LEU788
A	MET790
A	ASP855
A	PHE856
A	LEU858
A	ANP1102

site_id	AC4
Number of Residues	4
Details	binding site for residue MG B 1101

Chain	Residue
B	ASN842
B	ASP855
B	ANP1102
B	HOH1202

site_id	AC5
Number of Residues	17
Details	binding site for residue ANP B 1102

Chain	Residue
B	GLY721
B	ALA722
B	VAL726
B	ALA743
B	LYS745
B	MET790
B	GLN791
B	MET793
B	CYS797
B	ASP837
B	ARG841
B	ASN842
B	LEU844
B	ASP855
B	MG1101
B	HOH1201
B	HOH1202

site_id	AC6
Number of Residues	3
Details	binding site for residue MG C 1101

Chain	Residue
C	ASN842
C	ASP855
C	ANP1102

site_id	AC7
Number of Residues	16
Details	binding site for residue ANP C 1102

Chain	Residue
C	LEU718
C	GLY721
C	ALA722
C	VAL726
C	ALA743
C	LYS745
C	MET790
C	GLN791
C	MET793
C	ASP837
C	ARG841
C	ASN842
C	LEU844
C	ASP855
C	MG1101
C	9LL1103

site_id	AC8
Number of Residues	14
Details	binding site for residue 9LL C 1103

Chain	Residue
C	ALA743
C	ILE744
C	LYS745
C	GLU762
C	MET766
C	CYS775
C	ARG776
C	LEU777
C	LEU788
C	MET790
C	ASP855
C	PHE856
C	LEU858
C	ANP1102

site_id	AC9
Number of Residues	4
Details	binding site for residue MG D 1101

Chain	Residue
D	ASN842
D	ASP855
D	ANP1102
D	HOH1201

site_id	AD1
Number of Residues	19
Details	binding site for residue ANP D 1102

Chain	Residue
D	ALA722
D	VAL726
D	ALA743
D	LYS745
D	MET790
D	GLN791
D	MET793
D	CYS797
D	ASP837
D	ARG841
D	ASN842
D	LEU844
D	ASP855
D	MG1101
D	9LL1103
D	HOH1201
D	GLY719
D	SER720
D	GLY721

site_id	AD2
Number of Residues	14
Details	binding site for residue 9LL D 1103

Chain	Residue
D	ALA743
D	ILE744
D	LYS745
D	ILE759
D	MET766
D	CYS775
D	ARG776
D	LEU777
D	LEU788
D	MET790
D	ASP855
D	PHE856
D	LEU858
D	ANP1102

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	LEU718-LYS745

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

Chain	Residue	Details
A	LEU833-VAL845

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000255\|PROSITE-ProRule:PRU00159, ECO:0000255\|PROSITE-ProRule:PRU10028

Chain	Residue	Details
A	ASP837
B	ASP837
C	ASP837
D	ASP837

site_id	SWS_FT_FI2
Number of Residues	4
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
D	LEU718
A	LEU718
B	LEU718
C	LEU718

site_id	SWS_FT_FI3
Number of Residues	4
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
D	LYS745
A	LYS745
B	LYS745
C	LYS745

site_id	SWS_FT_FI4
Number of Residues	4
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
D	MET790
A	MET790
B	MET790
C	MET790

site_id	SWS_FT_FI5
Number of Residues	4
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
D	ASP855
A	ASP855
B	ASP855
C	ASP855

site_id	SWS_FT_FI6
Number of Residues	4
Details	SITE: Important for interaction with PIK3C2B

Chain	Residue	Details
D	TYR1016
A	TYR1016
B	TYR1016
C	TYR1016

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269\|PubMed:29192674

Chain	Residue	Details
B	LYS745
C	LYS745
D	LYS745
A	LYS745

site_id	SWS_FT_FI8
Number of Residues	4
Details	MOD_RES: Phosphotyrosine => ECO:0000269\|PubMed:23774213

Chain	Residue	Details
A	TYR869
B	TYR869
C	TYR869
D	TYR869

site_id	SWS_FT_FI9
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000269\|PubMed:16083266, ECO:0007744\|PubMed:18669648, ECO:0007744\|PubMed:20068231, ECO:0007744\|PubMed:24275569

Chain	Residue	Details
A	SER991
B	SER991
C	SER991
D	SER991

site_id	SWS_FT_FI10
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18669648

Chain	Residue	Details
A	SER995
B	SER995
C	SER995
D	SER995

site_id	SWS_FT_FI11
Number of Residues	4
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269\|PubMed:19563760, ECO:0007744\|PubMed:18669648

Chain	Residue	Details
A	TYR998
B	TYR998
C	TYR998
D	TYR998

site_id	SWS_FT_FI12
Number of Residues	4
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269\|PubMed:19563760, ECO:0000269\|PubMed:23774213

Chain	Residue	Details
B	TYR1016
A	TYR1016
C	TYR1016
D	TYR1016

site_id	SWS_FT_FI13
Number of Residues	16
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	LYS716
A	LYS737
C	LYS716
D	LYS867
A	LYS754
A	LYS867
B	LYS716
B	LYS737
B	LYS754
B	LYS867
C	LYS737
C	LYS754
C	LYS867
D	LYS716
D	LYS737
D	LYS754

site_id	SWS_FT_FI14
Number of Residues	12
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269\|PubMed:16543144

Chain	Residue	Details
A	LYS929
A	LYS970
B	LYS929
B	LYS970
C	LYS929
C	LYS970
D	LYS929
D	LYS970

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:33996800

Chain	Residue	Details
A	LYS757
A	LYS960
B	LYS757
B	LYS960
C	LYS757
C	LYS960
D	LYS757
D	LYS960

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)