7SYE: Extracellular module of the full-length EGFR

Cryo-EM structure of the extracellular module of the full-length EGFR bound to EGF. "tips-separated" 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: 281.32 kDa
Released: 22 Dec 2021

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

Secondary structure: helices and β-sheets

7SYE contains 34 α-helices and 121 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: 17 helices, 53 β-strands

Element	Residues	Length	Sheet
β-strand	6-7	2	1
α-helix	20-31	12
β-strand	36-37	2	1
β-strand	41-44	4	2
α-helix	53-57	5
β-strand	60-61	2	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	110	1	3
β-strand	118-119	2	1
β-strand	123-127	5	2
β-strand	144	1	1
α-helix	148-150	3
β-strand	153	1	2
α-helix	165-167	3
α-helix	171-173	3
α-helix	204-206	3
α-helix	207-209	3
β-strand	212	1	4
β-strand	216	1	5
β-strand	224	1	5
β-strand	227	1	4
β-strand	232	1	6
β-strand	235	1	6
α-helix	240-242	3
β-strand	244-247	4	7
β-strand	252-255	4	7
β-strand	261-262	2	8
β-strand	267-268	2	8
β-strand	276-277	2	9
β-strand	283-284	2	9
β-strand	293-296	4	10
β-strand	299-302	4	10
α-helix	309-311	3
β-strand	313-314	2	11
β-strand	317	1	12
β-strand	321	1	12
α-helix	333-335	3
β-strand	341-342	2	11
β-strand	345-347	3	13
α-helix	349-353	5
α-helix	360-364	5
α-helix	367-373	7
β-strand	377	1	11
β-strand	381-383	3	13
α-helix	394-396	3
β-strand	401-402	2	11
β-strand	408	1	13
β-strand	412-417	6	13
β-strand	431-432	2	11
β-strand	436-440	5	13
α-helix	453-455	3
β-strand	457	1	11
β-strand	464-467	4	13
α-helix	472-474	3
α-helix	476-478	3
β-strand	486	1	14
β-strand	491	1	15
β-strand	499	1	15
β-strand	502	1	14
β-strand	505-507	3	16
β-strand	510-512	3	16
β-strand	524-525	2	17
β-strand	530	1	16
β-strand	532-533	2	17
β-strand	573-575	3	18
β-strand	583-584	2	18

Chain B: 14 helices, 60 β-strands

Element	Residues	Length	Sheet
β-strand	6-7	2	19
α-helix	20-30	11
β-strand	36-37	2	19
β-strand	41-44	4	20
α-helix	46-47	2
β-strand	60-61	2	19
β-strand	65-68	4	20
β-strand	74	1	21
β-strand	82-83	2	19
β-strand	89	1	20
β-strand	93-98	6	20
β-strand	110	1	21
β-strand	118-119	2	19
β-strand	123-127	5	20
α-helix	140-143	4
β-strand	144	1	19
β-strand	153	1	20
β-strand	175	1	22
β-strand	183	1	22
β-strand	199	1	23
β-strand	207	1	23
α-helix	208-209	2
β-strand	216	1	24
β-strand	224	1	24
α-helix	240-242	3
β-strand	244-247	4	25
β-strand	252-255	4	25
β-strand	261-263	3	26
β-strand	266-268	3	26
β-strand	276-277	2	27
β-strand	283-284	2	27
β-strand	291-293	3	28
β-strand	302-304	3	28
β-strand	312-314	3	29
β-strand	318	1	30
β-strand	321	1	30
α-helix	330-335	6
β-strand	340-342	3	29
β-strand	345-347	3	31
α-helix	350-353	4
α-helix	360-364	5
α-helix	365-372	8
β-strand	376-377	2	29
β-strand	381-383	3	31
β-strand	392	1	32
β-strand	401-402	2	29
β-strand	408	1	33
β-strand	412	1	33
β-strand	414-417	4	31
β-strand	423	1	32
β-strand	431-432	2	29
β-strand	437-440	4	31
α-helix	453-455	3
β-strand	457	1	29
β-strand	464-467	4	31
α-helix	476-478	3
β-strand	505-506	2	34
β-strand	511-512	2	34
β-strand	524-527	4	35
β-strand	530-533	4	35
α-helix	534-535	2
β-strand	538	1	36
β-strand	547	1	37
α-helix	552-554	3
β-strand	555	1	37
β-strand	558	1	36
β-strand	561-563	3	38
β-strand	566-568	3	38
β-strand	573	1	39
α-helix	578-580	3
β-strand	584	1	39
β-strand	585-587	3	40
β-strand	592	1	38
β-strand	593-595	3	40

Chain C: 2 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	8-10	3
β-strand	21-23	3	41
β-strand	28-30	3	41
β-strand	37-38	2	42
β-strand	44-45	2	42
α-helix	47-49	3

Chain D: 1 helix, 4 β-strands

Element	Residues	Length	Sheet
α-helix	8-10	3
β-strand	21-23	3	43
β-strand	28-30	3	43
β-strand	37-38	2	44
β-strand	44-45	2	44

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

>7SYE_1 Epidermal growth factor receptor (chains A, B)
MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEV
VLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALA
VLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDF
QNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGC
TGPRESDCLVCRKFRNEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYV
VTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEFKDSLSINATNIKHFK
NCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAF
ENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKL
FGTSGQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCN
LLEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVM
GENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNGPKIPSIATGMVGALLLLLVV
ALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLRILKETEFKKIKVLGS
GAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGI
CLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAA
RNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSY
GVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPK
FRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQ
QGFFSSPSTSRTPLLSSLSATSNNSTVACIDRNGLQSCPIKEDSFLQRYSSDPTGALTED
SIDDTFLPVPEYINQSVPKRPAGSVQNPVYHNQPLNPAPSRDPHYQDPHSTAVGNPEYLN
TVQPTCVNSTFDSPAHWAQKGSHQISLDNPDYQQDFFPKEAKPNGIFKGSTAENAEYLRV
APQSSEFIGA

Sequence of entity 2 (C, D), FASTA

>7SYE_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

About this viewer

MolViewer shows 7SYE directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.