Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3LZB

EGFR kinase domain complexed with an imidazo[2,1-b]thiazole inhibitor

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	19
Details	BINDING SITE FOR RESIDUE ITI A 1

Chain	Residue
A	LEU694
A	LEU768
A	MET769
A	PRO770
A	PHE771
A	GLY772
A	CYS773
A	LEU820
A	THR830
A	PHE832
A	LEU834
A	VAL702
A	ALA719
A	LYS721
A	MET742
A	CYS751
A	LEU753
A	THR766
A	GLN767

site_id	AC2
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ITI B 1

Chain	Residue
B	LEU694
B	VAL702
B	ALA719
B	LYS721
B	MET742
B	CYS751
B	LEU753
B	THR766
B	GLN767
B	MET769
B	PRO770
B	PHE771
B	GLY772
B	CYS773
B	LEU820
B	THR830
B	ASP831
B	PHE832

site_id	AC3
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ITI C 1

Chain	Residue
C	LEU694
C	VAL702
C	ALA719
C	LYS721
C	MET742
C	CYS751
C	LEU753
C	THR766
C	GLN767
C	LEU768
C	MET769
C	GLY772
C	ASP776
C	LEU820
C	THR830
C	ASP831
C	PHE832
C	LEU834

site_id	AC4
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ITI D 1

Chain	Residue
D	LEU694
D	VAL702
D	ALA719
D	LYS721
D	MET742
D	CYS751
D	LEU753
D	LEU764
D	THR766
D	GLN767
D	LEU768
D	MET769
D	PRO770
D	GLY772
D	LEU820
D	THR830
D	PHE832
D	LEU834

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	8
Details	ACT_SITE: Proton acceptor => ECO:0000255\|PROSITE-ProRule:PRU00159, ECO:0000255\|PROSITE-ProRule:PRU10028

Chain	Residue	Details
A	ASP813
B	ASP813
C	ASP813
D	ASP813
E	ASP-140
F	ASP-139
G	ASP-141
H	ASP-142

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
A	LEU694
B	LEU694
C	LEU694
D	LEU694
E	LEU-259
F	LEU-258
G	LEU-260
H	LEU-261

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
A	LYS721
B	LYS721
C	LYS721
D	LYS721
E	LYS-232
F	LYS-231
G	LYS-233
H	LYS-234

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
A	THR766
B	THR766
C	THR766
D	THR766
E	THR-187
F	THR-186
G	THR-188
H	THR-189

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
A	ASP831
B	ASP831
C	ASP831
D	ASP831
E	ASP-122
F	ASP-121
G	ASP-123
H	ASP-124

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

Chain	Residue	Details
A	UNK992
B	UNK992
C	UNK992
D	UNK992
E	UNK39
F	UNK40
G	UNK38
H	UNK37

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

Chain	Residue	Details
A	LYS721
B	LYS721
C	LYS721
D	LYS721
E	LYS-232
F	LYS-231
G	LYS-233
H	LYS-234

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

Chain	Residue	Details
A	TYR845
B	TYR845
C	TYR845
D	TYR845
E	TYR-108
F	TYR-107
G	TYR-109
H	TYR-110

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
A	UNK967
B	UNK967
C	UNK967
D	UNK967
E	UNK14
F	UNK15
G	UNK13
H	UNK12

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

Chain	Residue	Details
A	UNK971
B	UNK971
C	UNK971
D	UNK971
E	UNK18
F	UNK19
G	UNK17
H	UNK16

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
A	UNK974
B	UNK974
C	UNK974
D	UNK974
E	UNK21
F	UNK22
G	UNK20
H	UNK19

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
A	UNK992
B	UNK992
C	UNK992
D	UNK992
E	UNK39
F	UNK40
G	UNK38
H	UNK37

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
A	LYS692
C	LYS713
C	LYS730
C	LYS843
D	LYS692
D	LYS713
D	LYS730
D	LYS843
E	LYS-261
E	LYS-240
E	LYS-223
A	LYS713
E	LYS-110
F	LYS-260
F	LYS-239
F	LYS-222
F	LYS-109
G	LYS-262
G	LYS-241
G	LYS-224
G	LYS-111
H	LYS-263
A	LYS730
H	LYS-242
H	LYS-225
H	LYS-112
A	LYS843
B	LYS692
B	LYS713
B	LYS730
B	LYS843
C	LYS692

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
D	LYS905
D	LYS946
E	LYS-48
E	LYS-7
F	LYS-47
F	LYS-6
A	LYS905
G	LYS-49
G	LYS-8
H	LYS-50
H	LYS-9
A	LYS946
B	LYS905
B	LYS946
C	LYS905
C	LYS946

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
A	LYS733
E	LYS-17
F	LYS-219
F	LYS-16
G	LYS-221
G	LYS-18
H	LYS-222
H	LYS-19
A	LYS936
B	LYS733
B	LYS936
C	LYS733
C	LYS936
D	LYS733
D	LYS936
E	LYS-220

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