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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5UGA

Crystal structure of the EGFR kinase domain (L858R, T790M, V948R) in complex with 4-(4-{[2-{[(3S)-1-acetylpyrrolidin-3-yl]amino}-9-(propan-2-yl)-9H-purin-6-yl]amino}phenyl)-1-methylpiperazin-1-ium

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	binding site for residue 8BM A 9001

Chain	Residue
A	LEU718
A	ASN842
A	LEU844
A	THR854
A	GLY719
A	SER720
A	VAL726
A	ALA743
A	GLN791
A	MET793
A	PRO794
A	GLY796

site_id	AC2
Number of Residues	7
Details	binding site for residue SO4 A 9002

Chain	Residue
A	ARG836
A	TYR869
A	ALA871
A	GLU872
A	GLY873
A	HOH9113
A	HOH9182

site_id	AC3
Number of Residues	3
Details	binding site for residue SO4 A 9003

Chain	Residue
A	ARG803
A	LYS913
A	HOH9131

site_id	AC4
Number of Residues	5
Details	binding site for residue GOL A 9004

Chain	Residue
A	SER752
A	ASN816
A	GLN820
A	LYS823
A	HOH9102

site_id	AC5
Number of Residues	8
Details	binding site for residue GOL A 9005

Chain	Residue
A	THR940
A	ILE941
A	ASP942
A	ARG977
A	TYR978
A	HOH9121
A	HOH9162
A	HOH9188

site_id	AC6
Number of Residues	4
Details	binding site for residue GOL A 9006

Chain	Residue
A	LEU747
A	ALA750
A	PRO753
A	LYS754

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	1
Details	ACT_SITE: Proton acceptor => ECO:0000255\|PROSITE-ProRule:PRU00159, ECO:0000255\|PROSITE-ProRule:PRU10028

Chain	Residue	Details
A	ASP837

site_id	SWS_FT_FI2
Number of Residues	1
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	LEU718

site_id	SWS_FT_FI3
Number of Residues	1
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	LYS745

site_id	SWS_FT_FI4
Number of Residues	1
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	MET790

site_id	SWS_FT_FI5
Number of Residues	1
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	ASP855

site_id	SWS_FT_FI6
Number of Residues	1
Details	SITE: Important for interaction with PIK3C2B

Chain	Residue	Details
A	TYR1016

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000269\|PubMed:3138233, ECO:0007744\|PubMed:18691976

Chain	Residue	Details
A	SER695

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269\|PubMed:29192674

Chain	Residue	Details
A	LYS745

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000269\|PubMed:23774213

Chain	Residue	Details
A	TYR869

site_id	SWS_FT_FI10
Number of Residues	1
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

site_id	SWS_FT_FI11
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18669648

Chain	Residue	Details
A	SER995

site_id	SWS_FT_FI12
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269\|PubMed:19563760, ECO:0007744\|PubMed:18669648

Chain	Residue	Details
A	TYR998

site_id	SWS_FT_FI13
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269\|PubMed:19563760, ECO:0000269\|PubMed:23774213

Chain	Residue	Details
A	TYR1016

site_id	SWS_FT_FI14
Number of Residues	4
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
A	LYS754
A	LYS867

site_id	SWS_FT_FI15
Number of Residues	3
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269\|PubMed:16543144

Chain	Residue	Details
A	LYS929
A	LYS970

site_id	SWS_FT_FI16
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269\|PubMed:33996800

Chain	Residue	Details
A	LYS757
A	LYS960

227344

PDB entries from 2024-11-13

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