8HGS: The EGF-bound EGFR ectodomain homodimer

The EGF-bound EGFR ectodomain homodimer. Determined by electron microscopy at 3.81 Å resolution. Released 15 Feb 2023.

Method: Electron microscopy
Resolution: 3.81 Å
Organism: Homo sapiens
Chains: 4
Atoms: 10,080
Mol. weight: 177.64 kDa
Ligands: NAG
Released: 15 Feb 2023

Explore 8HGS in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8HGS contains 36 α-helices and 146 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chains A and B: 16 helices, 69 β-strands

Element	Residues	Length	Sheet
β-strand	30-33	4	1
β-strand	40-41	2	2
α-helix	44-54	11
β-strand	60-64	5	1
β-strand	65-70	6	3
α-helix	77-81	5
β-strand	84-85	2	1
β-strand	89-94	6	3
β-strand	98	1	4
β-strand	106-107	2	1
β-strand	113	1	5
β-strand	117	1	5
β-strand	119-122	4	3
β-strand	134	1	4
β-strand	142-143	2	1
β-strand	148-151	4	3
β-strand	177	1	3
α-helix	195-197	3
β-strand	199	1	6
α-helix	204-206	3
β-strand	207	1	6
β-strand	223	1	7
β-strand	231	1	7
β-strand	236	1	8
β-strand	240	1	9
α-helix	245-247	3
β-strand	248	1	9
β-strand	251	1	8
β-strand	254-256	3	10
β-strand	259-261	3	10
β-strand	268-271	4	11
β-strand	276-279	4	11
α-helix	280	1
β-strand	285-287	3	12
β-strand	290-292	3	12
β-strand	300-301	2	13
β-strand	306	1	12
β-strand	307-308	2	13
β-strand	315-317	3	14
β-strand	326-328	3	14
α-helix	329	1
α-helix	336	1
β-strand	337-338	2	15
α-helix	343-345	3
α-helix	355-358	4
β-strand	365-366	2	15
β-strand	369-371	3	16
α-helix	373-377	5
β-strand	379	1	17
β-strand	384	1	17
α-helix	385-388	4
α-helix	390-397	8
β-strand	400-401	2	15
β-strand	405-407	3	16
β-strand	416	1	18
β-strand	425-426	2	15
β-strand	432	1	16
β-strand	436-440	5	16
β-strand	447	1	18
β-strand	455-456	2	15
β-strand	460-462	3	16
β-strand	481	1	15
β-strand	488	1	16
α-helix	499-501	3
β-strand	510	1	19
β-strand	515	1	20
β-strand	523	1	20
β-strand	526	1	19
β-strand	529-531	3	21
β-strand	534-536	3	21
β-strand	548-551	4	21
β-strand	554-557	4	21
β-strand	562	1	22
β-strand	571	1	23
α-helix	576-578	3
β-strand	579	1	23
β-strand	582	1	22
β-strand	585-587	3	24
β-strand	590-592	3	24
β-strand	597-599	3	25
α-helix	606	1
β-strand	607-608	2	25
β-strand	610	1	26
β-strand	616	1	24
β-strand	618	1	26

Chains C and D: 2 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	8-10	3
α-helix	18	1
β-strand	19-23	5	2
β-strand	28-33	6	2
β-strand	37-38	2	27
β-strand	44-45	2	27

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Epidermal growth factor receptor	A, B	protein	736	Homo sapiens	P00533 (AlphaFold model)
Pro-epidermal growth factor	C, D	protein	57	Homo sapiens	P01133 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>8HGS_1 Epidermal growth factor receptor (chains A, B)
MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEV
VLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALA
VLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDF
QNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGC
TGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYV
VTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEFKDSLSINATNIKHFK
NCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAF
ENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKL
FGTSGQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCN
LLEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVM
GENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNGPKIPSIATGMVGALLLLLVV
ALGIGLFMRRRHIVRKRTLRRLLGGSENLYFQGGGSAAQLKKKLQALKKKNAQLKWKLQA
LKKKLAQSNSLEVLFQ

Sequence of entity 2 (C, D), FASTA

>8HGS_2 Pro-epidermal growth factor (chains C, D)
GPTANSDSECPLSHDGYCLHDGVCMYIEALDKYACNCVVGYIGERCQYRDLKWWELR

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	4

Primary citation

Structure and dynamics of the EGFR/HER2 heterodimer. Bai, X., Sun, P., Wang, X. et al. Cell Discov (2023) 9:18-18. DOI 10.1038/s41421-023-00523-5 · PubMed

Other PDB entries of the same protein (UniProt P00533 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8A27 1.07 Å, EGFR kinase domain in complex with 2-(6,7-dihydro-5H-pyrrolo[1,2-c]imidazol-1-yl)-2-[6-[2…
8A2D 1.11 Å, EGFR kinase domain (L858R/V948R) in complex with 2-[4-(difluoromethyl)-6-[2-[4-[[4-(hydro…
5UG9 1.33 Å, Crystal structure of the EGFR kinase domain (L858R, T790M, V948R) in complex with a…
5HG8 1.42 Å, EGFR (L858R, T790M, V948R) in complex with N-[3-({2-[(1-methyl-1H-pyrazol-4-yl)amino]-7H-…
8A2A 1.43 Å, EGFR kinase domain in complex with 2-(6,7-dihydro-5H-pyrrolo[1,2-c]imidazol-1-yl)-2-[6-[2…
5UG8 1.46 Å, Crystal structure of the EGFR kinase domain (L858R, T790M, V948R) in complex with a…
3POZ 1.5 Å, EGFR Kinase domain complexed with tak-285
6TFV 1.5 Å, Crystal Structure of EGFR T790M/V948R in Complex with Covalent Pyrrolopyrimidine 18b
6TG0 1.5 Å, Crystal Structure of EGFR T790M/V948R in Complex with Covalent Pyrrolopyrimidine 21a
3VRP 1.52 Å, Crystal structure of the tyrosine kinase binding domain of Cbl-c in complex with…
5HG5 1.52 Å, EGFR (L858R, T790M, V948R) in complex with N-{3-[(2-{[4-(4-methylpiperazin-1-yl)phenyl]am…
5CNO 1.55 Å, Crystal structure of the EGFR kinase domain mutant V924R

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