7SZ5: Extracellular module of the full-length EGFR

Cryo-EM structure of the extracellular module of the full-length EGFR bound to TGF-alpha "tips-separated" conformation. Determined by electron microscopy at 3.6 Å resolution. Released 22 Dec 2021.

Method: Electron microscopy
Resolution: 3.6 Å
Organism: Homo sapiens
Chains: 4
Atoms: 9,367
Mol. weight: 279.99 kDa
Released: 22 Dec 2021

Explore 7SZ5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7SZ5 contains 30 α-helices and 107 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: 16 helices, 48 β-strands

Element	Residues	Length	Sheet
α-helix	4-5	2
β-strand	16-17	2	1
α-helix	20-31	12
β-strand	66-68	3	2
β-strand	74	1	3
β-strand	82-83	2	4
β-strand	89	1	2
β-strand	93-98	6	2
β-strand	110	1	3
β-strand	118-119	2	4
β-strand	123-126	4	2
α-helix	135-137	3
α-helix	140-143	4
α-helix	148-150	3
α-helix	163-167	5
α-helix	171-173	3
β-strand	212	1	5
β-strand	216	1	6
β-strand	224	1	6
β-strand	227	1	5
α-helix	240-242	3
β-strand	246	1	7
β-strand	253	1	7
β-strand	261-262	2	8
β-strand	267-268	2	8
β-strand	276-277	2	9
β-strand	282	1	8
β-strand	283-284	2	9
β-strand	294	1	10
β-strand	301	1	10
β-strand	313-314	2	11
β-strand	318	1	12
β-strand	321	1	12
β-strand	340-342	3	11
β-strand	345-347	3	13
β-strand	355	1	14
β-strand	360	1	14
α-helix	367-373	7
β-strand	376-377	2	11
β-strand	381-383	3	13
β-strand	401-402	2	11
β-strand	408	1	13
β-strand	412-417	6	13
β-strand	436-440	5	13
α-helix	447-449	3
α-helix	453-456	4
β-strand	464-465	2	13
α-helix	472-475	4
β-strand	491	1	15
β-strand	499	1	15
β-strand	505-507	3	16
β-strand	510-512	3	16
β-strand	525-527	3	16
β-strand	530-532	3	16
α-helix	533-535	3
α-helix	539-541	3
α-helix	552-554	3
β-strand	561	1	17
β-strand	568	1	17
β-strand	573-576	4	18
β-strand	582-584	3	18
β-strand	586-587	2	19
β-strand	593-594	2	19
α-helix	608-610	3

Chain B: 13 helices, 47 β-strands

Element	Residues	Length	Sheet
β-strand	6-7	2	22
β-strand	16-17	2	23
α-helix	20-30	11
β-strand	36-37	2	22
β-strand	41-44	4	24
α-helix	54-56	3
β-strand	60-61	2	22
β-strand	65-68	4	24
β-strand	74	1	25
β-strand	82-83	2	22
β-strand	89	1	24
β-strand	93-98	6	24
β-strand	110	1	25
β-strand	118-119	2	22
β-strand	123-126	4	24
α-helix	147-150	4
β-strand	153-154	2	24
α-helix	171-173	3
β-strand	175	1	26
β-strand	183	1	26
α-helix	207-209	3
β-strand	212	1	27
β-strand	216	1	28
β-strand	224	1	28
β-strand	227	1	27
α-helix	240-242	3
β-strand	244-246	3	29
β-strand	253-255	3	29
β-strand	261-262	2	30
β-strand	267-268	2	30
β-strand	276-277	2	31
β-strand	282	1	30
β-strand	283-284	2	31
β-strand	291-295	5	31
β-strand	300-304	5	31
α-helix	309-311	3
β-strand	314	1	32
α-helix	315	1
α-helix	332-334	3
β-strand	340-341	2	33
β-strand	342	1	32
β-strand	346-347	2	34
α-helix	361-364	4
α-helix	365-367	3
β-strand	376-377	2	33
β-strand	381-383	3	34
β-strand	393	1	35
β-strand	401-402	2	33
β-strand	408	1	36
β-strand	412	1	36
β-strand	414-416	3	34
β-strand	425	1	35
β-strand	431-432	2	33
β-strand	437-438	2	34
α-helix	453-455	3
β-strand	457	1	33
β-strand	465	1	34
α-helix	476-478	3
β-strand	491	1	37
β-strand	499	1	37

Chain C: 1 helix, 7 β-strands

Element	Residues	Length	Sheet
β-strand	5-6	2	20
β-strand	19-20	2	1
β-strand	23-24	2	20
β-strand	29-30	2	20
α-helix	32	1
β-strand	33-34	2	1
β-strand	38-39	2	21
β-strand	45-46	2	21

Chain D: 0 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	5-7	3	38
β-strand	22-24	3	38
β-strand	33-34	2	23
β-strand	38	1	39
β-strand	46	1	39

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Epidermal growth factor receptor	A, B	protein	1210	Homo sapiens	P00533 (AlphaFold model)
Transforming growth factor alpha	C, D	protein	50	Homo sapiens	P01135 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>7SZ5_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

>7SZ5_2 Transforming growth factor alpha (chains C, D)
VVSHFNDCPDSHTQFCFHGTCRFLVQEDKPACVCHSGYVGARCEHADLLA

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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