7SZ0: Epidermal growth factor receptor

Cryo-EM structure of the extracellular module of the full-length EGFR L834R bound to EGF. "tips-juxtaposed" conformation. Determined by electron microscopy at 3.3 Å resolution. Released 22 Dec 2021.

Method: Electron microscopy
Resolution: 3.3 Å
Organism: Homo sapiens
Chains: 4
Atoms: 10,216
Mol. weight: 281.41 kDa
Released: 22 Dec 2021

Explore 7SZ0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7SZ0 contains 34 α-helices and 126 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.

Chain A: 19 helices, 59 β-strands

Element	Residues	Length	Sheet
α-helix	4-5	2
β-strand	6-7	2	1
α-helix	20-31	12
β-strand	36-37	2	1
β-strand	41-42	2	2
α-helix	53-55	3
β-strand	61	1	1
β-strand	65-68	4	2
β-strand	74	1	3
β-strand	82-83	2	1
β-strand	89	1	2
β-strand	93-98	6	2
β-strand	101	1	4
β-strand	107	1	4
β-strand	110	1	3
β-strand	118-119	2	1
β-strand	123-127	5	2
α-helix	135-137	3
β-strand	144	1	1
α-helix	148-150	3
β-strand	153-154	2	2
β-strand	175	1	5
β-strand	183	1	5
α-helix	184-186	3
β-strand	199	1	6
α-helix	204-206	3
β-strand	207	1	6
α-helix	208-209	2
β-strand	216	1	7
β-strand	224	1	7
α-helix	240-242	3
β-strand	244-246	3	8
β-strand	253-255	3	8
β-strand	261-262	2	9
β-strand	267-268	2	9
β-strand	276-278	3	9
β-strand	282-284	3	9
β-strand	291-296	6	10
β-strand	299-304	6	10
β-strand	313-314	2	11
α-helix	333-335	3
β-strand	341-342	2	11
β-strand	345-347	3	12
α-helix	361-364	4
α-helix	365-373	9
β-strand	376-377	2	11
β-strand	381-383	3	12
α-helix	394-396	3
β-strand	401-402	2	11
β-strand	408	1	12
β-strand	412-417	6	12
β-strand	431-432	2	11
β-strand	436-440	5	12
α-helix	453-455	3
β-strand	457	1	11
β-strand	465	1	12
α-helix	474-478	5
β-strand	491	1	13
α-helix	496-498	3
β-strand	499	1	13
β-strand	505	1	14
β-strand	506	1	15
β-strand	512	1	14
β-strand	524-525	2	16
β-strand	530	1	15
β-strand	532-533	2	16
α-helix	534-535	2
β-strand	538	1	17
α-helix	539-540	2
β-strand	547	1	18
α-helix	552-554	3
β-strand	555	1	18
β-strand	558	1	17
β-strand	562-563	2	19
β-strand	566-567	2	19
β-strand	573-576	4	20
β-strand	582-584	3	20
β-strand	592	1	19

Chain B: 14 helices, 59 β-strands

Element	Residues	Length	Sheet
β-strand	6-7	2	23
α-helix	20-28	9
β-strand	36-37	2	23
β-strand	41-44	4	24
α-helix	53-57	5
β-strand	60-61	2	23
β-strand	65-68	4	24
β-strand	74	1	25
β-strand	82	1	26
β-strand	89	1	24
β-strand	93-97	5	24
β-strand	101	1	27
β-strand	107	1	27
β-strand	110	1	25
β-strand	118	1	26
β-strand	119	1	28
β-strand	123-129	7	24
α-helix	135-137	3
β-strand	144	1	28
β-strand	153-156	4	24
β-strand	175	1	29
β-strand	183	1	29
β-strand	212	1	30
β-strand	216	1	31
β-strand	224	1	31
β-strand	227	1	30
α-helix	240-242	3
β-strand	246-247	2	32
β-strand	252-253	2	32
β-strand	261-263	3	33
β-strand	266-268	3	33
β-strand	276-277	2	34
β-strand	282	1	33
β-strand	283-284	2	34
β-strand	291-296	6	34
β-strand	299-304	6	34
β-strand	313-314	2	35
α-helix	315	1
α-helix	319-321	3
α-helix	332-334	3
β-strand	340-342	3	35
β-strand	345-347	3	36
α-helix	361-364	4
α-helix	365-373	9
β-strand	376-377	2	35
β-strand	381-383	3	36
α-helix	394-396	3
β-strand	401-402	2	35
β-strand	408	1	36
β-strand	412-415	4	36
β-strand	431-432	2	35
β-strand	436-438	3	36
β-strand	457	1	35
β-strand	465	1	36
α-helix	472-476	5
β-strand	486	1	37
α-helix	496-498	3
β-strand	502	1	37
β-strand	505-506	2	38
β-strand	511-512	2	38
β-strand	524-527	4	39
β-strand	530-533	4	39
α-helix	534-535	2
β-strand	538	1	40
β-strand	558	1	40
β-strand	561-563	3	41
β-strand	566-568	3	41
β-strand	573	1	42
α-helix	578-580	3
β-strand	584	1	42
β-strand	585-587	3	43
β-strand	592	1	41
β-strand	593-595	3	43

Chain C: 1 helix, 4 β-strands

Element	Residues	Length	Sheet
α-helix	18-20	3
β-strand	21-23	3	21
β-strand	28-30	3	21
β-strand	37-38	2	22
β-strand	44-45	2	22

Chain D: 0 helices, 4 β-strands

Element	Residues	Length	Sheet
β-strand	21-23	3	44
β-strand	28-30	3	44
β-strand	37-38	2	45
β-strand	44-45	2	45

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Epidermal growth factor receptor	A, B	protein	1210	Homo sapiens	P00533 (AlphaFold model)
Epidermal growth factor	C, D	protein	53	Homo sapiens	P01133 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>7SZ0_1 Epidermal growth factor receptor (chains A, B)
MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEV
VLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALA
VLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDF
QNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGC
TGPRESDCLVCRKFRNEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYV
VTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEFKDSLSINATNIKHFK
NCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAF
ENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKL
FGTSGQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCN
LLEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVM
GENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNGPKIPSIATGMVGALLLLLVV
ALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLRILKETEFKKIKVLGS
GAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGI
CLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAA
RNVLVKTPQHVKITDFGRAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSY
GVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPK
FRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQ
QGFFSSPSTSRTPLLSSLSATSNNSTVACIDRNGLQSCPIKEDSFLQRYSSDPTGALTED
SIDDTFLPVPEYINQSVPKRPAGSVQNPVYHNQPLNPAPSRDPHYQDPHSTAVGNPEYLN
TVQPTCVNSTFDSPAHWAQKGSHQISLDNPDYQQDFFPKEAKPNGIFKGSTAENAEYLRV
APQSSEFIGA

Sequence of entity 2 (C, D), FASTA

>7SZ0_2 Epidermal growth factor (chains C, D)
NSDSECPLSHDGYCLHDGVCMYIEALDKYACNCVVGYIGERCQYRDLKWWELR

Primary citation

A molecular mechanism for the generation of ligand-dependent differential outputs by the epidermal growth factor receptor. Huang, Y., Ognjenovic, J., Karandur, D. et al. Elife (2021) 10. DOI 10.7554/eLife.73218 · 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

Browse structure collections

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