Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6V6O

EGFR(T790M/V948R) in complex with LN2380

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
E	0004672	molecular_function	protein kinase activity
E	0004713	molecular_function	protein tyrosine kinase activity
E	0005524	molecular_function	ATP binding
E	0006468	biological_process	protein phosphorylation
F	0004672	molecular_function	protein kinase activity
F	0004713	molecular_function	protein tyrosine kinase activity
F	0005524	molecular_function	ATP binding
F	0006468	biological_process	protein phosphorylation
G	0004672	molecular_function	protein kinase activity
G	0004713	molecular_function	protein tyrosine kinase activity
G	0005524	molecular_function	ATP binding
G	0006468	biological_process	protein phosphorylation
H	0004672	molecular_function	protein kinase activity
H	0004713	molecular_function	protein tyrosine kinase activity
H	0005524	molecular_function	ATP binding
H	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue CL D 1201

Chain	Residue
D	GLY721
D	ALA722
D	PHE723
D	LYS745
D	ARG841

site_id	AC2
Number of Residues	17
Details	binding site for residue QQM D 1202

Chain	Residue
D	LEU788
D	ILE789
D	MET790
D	GLN791
D	MET793
D	PRO794
D	GLY796
D	CYS797
D	ASP800
D	ARG841
D	LEU844
D	THR854
D	ASP855
D	LEU718
D	VAL726
D	ALA743
D	LYS745

site_id	AC3
Number of Residues	3
Details	binding site for residue CL A 1201

Chain	Residue
A	PHE723
A	LYS745
A	QQM1202

site_id	AC4
Number of Residues	5
Details	binding site for residue CL B 1201

Chain	Residue
B	GLY721
B	PHE723
B	LYS745
B	ARG841
B	HOH1350

site_id	AC5
Number of Residues	3
Details	binding site for residue CL C 1201

Chain	Residue
C	GLY721
C	PHE723
C	LYS745

site_id	AC6
Number of Residues	3
Details	binding site for residue CL E 1201

Chain	Residue
E	GLY721
E	PHE723
E	LYS745

site_id	AC7
Number of Residues	5
Details	binding site for residue CL F 1201

Chain	Residue
F	GLY721
F	PHE723
F	GLY724
F	LYS745
F	HOH1432

site_id	AC8
Number of Residues	4
Details	binding site for residue CL G 1302

Chain	Residue
G	GLY721
G	ALA722
G	PHE723
G	GLY724

site_id	AC9
Number of Residues	3
Details	binding site for residue CL H 1201

Chain	Residue
H	GLY721
H	PHE723
H	LYS745

site_id	AD1
Number of Residues	24
Details	binding site for Di-peptide QQM A 1202 and CYS A 797

Chain	Residue
A	LEU718
A	VAL726
A	ALA743
A	LYS745
A	LEU777
A	LEU788
A	ILE789
A	MET790
A	GLN791
A	MET793
A	GLY796
A	LEU798
A	LEU799
A	ASP800
A	TYR801
A	ARG841
A	ASN842
A	VAL843
A	LEU844
A	THR854
A	ASP855
A	CL1201
A	HOH1311
A	HOH1363

site_id	AD2
Number of Residues	20
Details	binding site for Di-peptide QQM B 1202 and CYS B 797

Chain	Residue
B	VAL726
B	ALA743
B	LYS745
B	LEU788
B	ILE789
B	MET790
B	GLN791
B	LEU792
B	MET793
B	GLY796
B	LEU798
B	LEU799
B	ASP800
B	TYR801
B	ARG841
B	VAL843
B	LEU844
B	THR854
B	ASP855
B	HOH1302

site_id	AD3
Number of Residues	25
Details	binding site for Di-peptide QQM C 1202 and CYS C 797

Chain	Residue
C	ILE789
C	MET790
C	GLN791
C	LEU792
C	MET793
C	PRO794
C	GLY796
C	LEU798
C	LEU799
C	ASP800
C	TYR801
C	ARG841
C	VAL843
C	LEU844
C	THR854
C	ASP855
C	HOH1302
C	HOH1382
C	LEU718
C	SER720
C	GLY721
C	VAL726
C	ALA743
C	LYS745
C	LEU788

site_id	AD4
Number of Residues	23
Details	binding site for Di-peptide QQM E 1202 and CYS E 797

Chain	Residue
E	LEU718
E	VAL726
E	ALA743
E	LYS745
E	LEU777
E	LEU788
E	ILE789
E	MET790
E	GLN791
E	MET793
E	PRO794
E	GLY796
E	LEU798
E	LEU799
E	ASP800
E	TYR801
E	ARG841
E	ASN842
E	VAL843
E	LEU844
E	THR854
E	ASP855
E	HOH1366

site_id	AD5
Number of Residues	23
Details	binding site for Di-peptide QQM F 1202 and CYS F 797

Chain	Residue
F	LEU718
F	VAL726
F	ALA743
F	LYS745
F	LEU777
F	LEU788
F	ILE789
F	MET790
F	GLN791
F	LEU792
F	MET793
F	PRO794
F	GLY796
F	LEU798
F	LEU799
F	ASP800
F	TYR801
F	ARG841
F	ASN842
F	VAL843
F	LEU844
F	ASP855
F	HOH1307

site_id	AD6
Number of Residues	22
Details	binding site for Di-peptide QQM G 1301 and CYS G 797

Chain	Residue
G	LEU718
G	VAL726
G	ALA743
G	LYS745
G	LEU788
G	ILE789
G	MET790
G	GLN791
G	LEU792
G	MET793
G	PRO794
G	GLY796
G	LEU798
G	LEU799
G	ASP800
G	TYR801
G	ARG841
G	ASN842
G	VAL843
G	LEU844
G	THR854
G	HOH1401

site_id	AD7
Number of Residues	25
Details	binding site for Di-peptide QQM H 1202 and CYS H 797

Chain	Residue
H	LEU718
H	SER720
H	VAL726
H	ALA743
H	LYS745
H	LEU777
H	LEU788
H	ILE789
H	MET790
H	GLN791
H	LEU792
H	MET793
H	PRO794
H	GLY796
H	LEU798
H	LEU799
H	ASP800
H	TYR801
H	ARG841
H	ASN842
H	VAL843
H	LEU844
H	THR854
H	ASP855
H	HOH1301

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
D	LEU718-LYS745

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

Chain	Residue	Details
D	LEU833-VAL845

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	ACT_SITE: Proton acceptor => ECO:0000255\|PROSITE-ProRule:PRU00159, ECO:0000255\|PROSITE-ProRule:PRU10028

Chain	Residue	Details
D	ASP837
A	ASP837
B	ASP837
C	ASP837
E	ASP837
F	ASP837
G	ASP837
H	ASP837

site_id	SWS_FT_FI2
Number of Residues	8
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
E	LEU718
F	LEU718
G	LEU718
H	LEU718

site_id	SWS_FT_FI3
Number of Residues	8
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
E	LYS745
F	LYS745
G	LYS745
H	LYS745

site_id	SWS_FT_FI4
Number of Residues	8
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
E	MET790
F	MET790
G	MET790
H	MET790

site_id	SWS_FT_FI5
Number of Residues	8
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
E	ASP855
F	ASP855
G	ASP855
H	ASP855

site_id	SWS_FT_FI6
Number of Residues	8
Details	SITE: Important for interaction with PIK3C2B

Chain	Residue	Details
D	TYR1016
A	TYR1016
B	TYR1016
C	TYR1016
E	TYR1016
F	TYR1016
G	TYR1016
H	TYR1016

site_id	SWS_FT_FI7
Number of Residues	8
Details	MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269\|PubMed:29192674

Chain	Residue	Details
D	LYS745
A	LYS745
B	LYS745
C	LYS745
E	LYS745
F	LYS745
G	LYS745
H	LYS745

site_id	SWS_FT_FI8
Number of Residues	8
Details	MOD_RES: Phosphotyrosine => ECO:0000269\|PubMed:23774213

Chain	Residue	Details
D	TYR869
A	TYR869
B	TYR869
C	TYR869
E	TYR869
F	TYR869
G	TYR869
H	TYR869

site_id	SWS_FT_FI9
Number of Residues	8
Details	MOD_RES: Phosphoserine => ECO:0000269\|PubMed:16083266, ECO:0007744\|PubMed:18669648, ECO:0007744\|PubMed:20068231, ECO:0007744\|PubMed:24275569

Chain	Residue	Details
D	SER991
A	SER991
B	SER991
C	SER991
E	SER991
F	SER991
G	SER991
H	SER991

site_id	SWS_FT_FI10
Number of Residues	8
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18669648

Chain	Residue	Details
D	SER995
A	SER995
B	SER995
C	SER995
E	SER995
F	SER995
G	SER995
H	SER995

site_id	SWS_FT_FI11
Number of Residues	8
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269\|PubMed:19563760, ECO:0007744\|PubMed:18669648

Chain	Residue	Details
D	TYR998
A	TYR998
B	TYR998
C	TYR998
E	TYR998
F	TYR998
G	TYR998
H	TYR998

site_id	SWS_FT_FI12
Number of Residues	8
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269\|PubMed:19563760, ECO:0000269\|PubMed:23774213

Chain	Residue	Details
D	TYR1016
A	TYR1016
B	TYR1016
C	TYR1016
E	TYR1016
F	TYR1016
G	TYR1016
H	TYR1016

site_id	SWS_FT_FI13
Number of Residues	32
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269\|PubMed:16543144, ECO:0000269\|PubMed:33996800

Chain	Residue	Details
D	LYS716
B	LYS737
B	LYS754
B	LYS867
C	LYS716
C	LYS737
C	LYS754
C	LYS867
E	LYS716
E	LYS737
E	LYS754
D	LYS737
E	LYS867
F	LYS716
F	LYS737
F	LYS754
F	LYS867
G	LYS716
G	LYS737
G	LYS754
G	LYS867
H	LYS716
D	LYS754
H	LYS737
H	LYS754
H	LYS867
D	LYS867
A	LYS716
A	LYS737
A	LYS754
A	LYS867
B	LYS716

site_id	SWS_FT_FI14
Number of Residues	24
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269\|PubMed:16543144

Chain	Residue	Details
C	LYS929
C	LYS970
E	LYS929
E	LYS970
F	LYS929
F	LYS970
D	LYS929
G	LYS929
G	LYS970
H	LYS929
H	LYS970
D	LYS970
A	LYS929
A	LYS970
B	LYS929
B	LYS970

site_id	SWS_FT_FI15
Number of Residues	16
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269\|PubMed:33996800

Chain	Residue	Details
D	LYS757
E	LYS960
F	LYS757
F	LYS960
G	LYS757
G	LYS960
H	LYS757
H	LYS960
D	LYS960
A	LYS757
A	LYS960
B	LYS757
B	LYS960
C	LYS757
C	LYS960
E	LYS757

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