8HGO: The EGF-bound EGFR/HER2 ectodomain complex

The EGF-bound EGFR/HER2 ectodomain complex. Determined by electron microscopy at 3.31 Å resolution. Released 8 Feb 2023.

Method: Electron microscopy
Resolution: 3.31 Å
Organism: Homo sapiens
Chains: 3
Atoms: 9,227
Mol. weight: 171.4 kDa
Ligands: NAG
Released: 8 Feb 2023

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

Secondary structure: helices and β-sheets

8HGO contains 29 α-helices and 124 β-strands across 3 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.

Chain A: 11 helices, 57 β-strands

Element	Residues	Length	Sheet
β-strand	30-31	2	25
β-strand	40-41	2	26
α-helix	44-54	11
β-strand	60-61	2	25
β-strand	65-68	4	27
α-helix	77-81	5
β-strand	84-85	2	25
β-strand	89-92	4	27
β-strand	98	1	28
β-strand	106-107	2	25
β-strand	119-122	4	27
β-strand	134	1	28
β-strand	142-143	2	25
β-strand	148-151	4	27
β-strand	168	1	25
β-strand	177-178	2	27
α-helix	195-197	3
β-strand	199	1	29
β-strand	207	1	29
β-strand	223	1	30
β-strand	231	1	30
β-strand	236-240	5	31
β-strand	248-251	4	31
β-strand	254-256	3	32
β-strand	259-261	3	32
β-strand	269	1	33
β-strand	278	1	33
β-strand	287	1	32
β-strand	290	1	32
β-strand	300-301	2	32
β-strand	307-308	2	32
β-strand	316-317	2	34
β-strand	325	1	32
β-strand	326-327	2	34
β-strand	337	1	35
β-strand	340	1	36
α-helix	343-345	3
α-helix	356-359	4
β-strand	364-365	2	35
β-strand	368	1	36
β-strand	369-371	3	37
α-helix	374-377	4
β-strand	379	1	38
β-strand	384	1	38
α-helix	385-388	4
α-helix	389-396	8
β-strand	400-401	2	35
β-strand	405-407	3	37
β-strand	416	1	39
α-helix	418-420	3
β-strand	425-426	2	35
β-strand	432	1	37
β-strand	436-440	5	37
β-strand	447	1	39
β-strand	455-456	2	35
β-strand	460-464	5	37
α-helix	477-479	3
β-strand	481	1	35
β-strand	488-491	4	37
β-strand	515	1	40
α-helix	520-522	3
β-strand	523	1	40
β-strand	548-549	2	41
β-strand	556-557	2	41
β-strand	562	1	42
β-strand	582	1	42
β-strand	585-587	3	43
β-strand	590-592	3	43

Chain B: 16 helices, 63 β-strands

Element	Residues	Length	Sheet
β-strand	25-26	2	1
α-helix	34-36	3
α-helix	42-50	9
β-strand	55-56	2	1
β-strand	60-63	4	2
α-helix	72-74	3
β-strand	79-80	2	1
β-strand	84-87	4	2
β-strand	93	1	3
β-strand	101-102	2	1
β-strand	114-117	4	2
β-strand	139	1	3
β-strand	148	1	1
β-strand	153-156	4	2
α-helix	169-172	4
β-strand	173	1	1
β-strand	182-184	3	2
β-strand	204	1	4
α-helix	209-211	3
β-strand	212	1	4
α-helix	213-215	3
β-strand	227	1	5
β-strand	235	1	5
α-helix	236-237	2
β-strand	240	1	6
β-strand	244	1	7
β-strand	252	1	7
β-strand	255	1	6
β-strand	258-260	3	8
β-strand	263-265	3	8
β-strand	272-275	4	9
β-strand	280-283	4	9
β-strand	289-291	3	8
β-strand	294-296	3	8
β-strand	304	1	10
β-strand	305	1	11
β-strand	310	1	8
β-strand	312	1	10
β-strand	319-320	2	12
β-strand	323	1	13
β-strand	329	1	13
β-strand	330	1	11
β-strand	332-333	2	12
β-strand	343	1	14
β-strand	345	1	15
α-helix	362-364	3
β-strand	369-370	2	16
β-strand	371	1	14
β-strand	373	1	15
β-strand	374-376	3	17
α-helix	383	1
β-strand	384	1	18
β-strand	389	1	18
α-helix	390-392	3
α-helix	397-400	4
β-strand	405-406	2	16
β-strand	410-412	3	17
α-helix	423-425	3
β-strand	430-431	2	16
β-strand	437	1	19
β-strand	441	1	19
β-strand	443-446	4	17
β-strand	460-461	2	16
β-strand	466-469	4	17
β-strand	493-496	4	17
α-helix	502-505	4
β-strand	515	1	20
α-helix	516-518	3
β-strand	520	1	21
β-strand	528	1	21
β-strand	531	1	20
β-strand	535	1	22
β-strand	540	1	22
β-strand	553-555	3	23
β-strand	560-562	3	23
β-strand	567	1	24
α-helix	568-570	3
α-helix	581-583	3
β-strand	587	1	24

Chain C: 2 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	8-10	3
α-helix	18	1
β-strand	19-23	5	26
β-strand	28-33	6	26
β-strand	37-38	2	44
β-strand	44-45	2	44

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Receptor tyrosine-protein kinase erbB-2	B	protein	745	Homo sapiens	P04626 (AlphaFold model)
Epidermal growth factor receptor	A	protein	736	Homo sapiens	P00533 (AlphaFold model)
Epidermal growth factor	C	protein	57	Homo sapiens	P01133 (AlphaFold model)

Sequence of entity 1 (B), FASTA

>8HGO_1 Receptor tyrosine-protein kinase erbB-2 (chains B)
MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL
ELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNG
DPLNNTTPVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQLA
LTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQC
AAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTACP
YNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSAN
IQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSLP
DLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHTV
PWDQLFRNPHQALLHTANRPEDECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQEC
VEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVARC
PSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSCVDLDDKGCPAEQRASPLTSIISAVVG
ILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQEGGSENLYFQGGGSAQLEKELQALEKEN
AQLEWELQALEKELAQSNSLEVLFQ

Sequence of entity 2 (A), FASTA

>8HGO_2 Epidermal growth factor receptor (chains A)
MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEV
VLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALA
VLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDF
QNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGC
TGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYV
VTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEFKDSLSINATNIKHFK
NCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAF
ENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKL
FGTSGQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCN
LLEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVM
GENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNGPKIPSIATGMVGALLLLLVV
ALGIGLFMRRRHIVRKRTLRRLLGGSENLYFQGGGSAAQLKKKLQALKKKNAQLKWKLQA
LKKKLAQSNSLEVLFQ

Sequence of entity 3 (C), FASTA

>8HGO_3 Epidermal growth factor (chains C)
GPTANSDSECPLSHDGYCLHDGVCMYIEALDKYACNCVVGYIGERCQYRDLKWWELR

Ligands and cofactors

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

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 P04626 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1MFG 1.25 Å, The Structure of ERBIN PDZ domain bound to the Carboxy-terminal tail of the ErbB2 Receptor
8VB5 1.48 Å, Crystal structure of kinase domain of HER2 Exon 20 insertion mutant in complex with…
8JYR 1.69 Å, Crystal structure of anti-HER2 antibody H2Mab-119 in complex with HER2 domain I
8U8X 1.69 Å, crystal structure of the receptor tyrosine kinase Human HER2 (ERBB2) YVMA mutant kinase…
8JYQ 1.75 Å, Crystal structure of cancer-specific anti-HER2 antibody H2Mab-214 in complex with…
7PCD 1.77 Å, HER2 in complex with a covalent inhibitor
5TQS 1.88 Å, Phospholipase C gamma-1 C-terminal SH2 domain bound to a phosphopeptide derived from the…
1MFL 1.88 Å, The Structure of ERBIN PDZ domain bound to the Carboxy-terminal tail of the ErbB2 Receptor
4GFU 2.0 Å, PTPN18 in complex with HER2-pY1248 phosphor-peptides
6LBX 2.03 Å, Crystal structure of HER2 Domain IV and Rb-H2
9IUT 2.09 Å, Crystal structure of cancer-specific anti-HER2 antibody H2Mab-250 in complex with…
5MY6 2.25 Å, Crystal structure of a HER2-Nb complex

Browse structure collections

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