1MOX: Human Epidermal Growth Factor Receptor

Crystal Structure of Human Epidermal Growth Factor Receptor (residues 1-501) in complex with TGF-alpha. Determined by X-ray diffraction at 2.5 Å resolution. Released 10 Sept 2003.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Homo sapiens
Chains: 4
Atoms: 8,686
Mol. weight: 127.95 kDa
Ligands: PT, CD, NAG
Released: 10 Sept 2003

Explore 1MOX in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1MOX contains 42 α-helices and 119 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: 23 helices, 53 β-strands

Element	Residues	Length	Sheet
β-strand	6-7	2	1
β-strand	10	1	2
β-strand	16	1	3
α-helix	20-31	12
β-strand	36-37	2	1
β-strand	40	1	2
β-strand	41-44	4	4
α-helix	53-57	5
β-strand	60-61	2	1
β-strand	65-68	4	4
β-strand	74	1	5
β-strand	82-83	2	1
β-strand	89	1	4
β-strand	93-98	6	4
β-strand	101	1	6
β-strand	107	1	6
β-strand	110	1	5
β-strand	118-119	2	1
β-strand	123-127	5	4
α-helix	135-137	3
α-helix	140-142	3
β-strand	144	1	1
α-helix	146-149	4
α-helix	163-167	5
α-helix	171-173	3
β-strand	175	1	7
α-helix	180-182	3
β-strand	183	1	7
α-helix	184-186	3
β-strand	199	1	8
β-strand	207	1	8
α-helix	208-209	2
β-strand	212-216	5	9
β-strand	224-227	4	9
β-strand	230-232	3	10
β-strand	235-237	3	10
α-helix	240-242	3
β-strand	244-247	4	11
β-strand	252-255	4	11
α-helix	256	1
β-strand	261-263	3	10
β-strand	266-268	3	10
β-strand	276-277	2	12
α-helix	278	1
β-strand	282	1	10
β-strand	283-284	2	12
β-strand	294	1	12
β-strand	301	1	12
β-strand	312-314	3	13
β-strand	316	1	14
α-helix	319-321	3
α-helix	331-333	3
β-strand	340-342	3	13
β-strand	344	1	14
β-strand	345-347	3	15
α-helix	350-353	4
β-strand	355	1	16
α-helix	356-358	3
β-strand	360	1	16
α-helix	365-373	9
β-strand	376-377	2	13
β-strand	381-383	3	15
α-helix	394-396	3
β-strand	401-402	2	13
β-strand	408	1	15
β-strand	412-417	6	15
β-strand	431-432	2	13
β-strand	436-440	5	15
α-helix	448-450	3
α-helix	453-456	4
β-strand	457	1	13
β-strand	464-465	2	15
α-helix	472-477	6
β-strand	491	1	17
α-helix	496-498	3
β-strand	499	1	17

Chain B: 18 helices, 55 β-strands

Element	Residues	Length	Sheet
β-strand	6-7	2	18
β-strand	10	1	19
β-strand	16-17	2	20
α-helix	20-31	12
β-strand	36-37	2	18
β-strand	40	1	19
β-strand	41-44	4	21
α-helix	46-47	2
α-helix	53-55	3
β-strand	60-61	2	18
β-strand	65-68	4	21
β-strand	74	1	22
β-strand	82-83	2	18
β-strand	89	1	21
β-strand	93-98	6	21
β-strand	101	1	23
β-strand	107	1	23
β-strand	110	1	22
β-strand	118	1	18
β-strand	119	1	24
β-strand	123-127	5	21
α-helix	135-137	3
β-strand	144	1	24
β-strand	153	1	21
α-helix	160-162	3
α-helix	164-165	2
β-strand	175	1	25
α-helix	180-182	3
β-strand	183	1	25
β-strand	199	1	26
β-strand	207	1	26
β-strand	212-216	5	27
β-strand	224-227	4	27
β-strand	230-232	3	28
β-strand	235-237	3	28
α-helix	240-242	3
β-strand	244-247	4	29
β-strand	252-255	4	29
β-strand	261-263	3	28
β-strand	266-268	3	28
β-strand	276-277	2	30
β-strand	282	1	28
β-strand	283-284	2	30
β-strand	291-297	7	30
β-strand	299-304	6	30
α-helix	310-311	2
β-strand	312-314	3	31
α-helix	319-321	3
α-helix	329-332	4
β-strand	340-342	3	31
β-strand	345-347	3	32
α-helix	350-353	4
β-strand	355	1	33
β-strand	360	1	33
α-helix	365-373	9
β-strand	376-377	2	31
β-strand	381-383	3	32
β-strand	392	1	34
α-helix	394-396	3
β-strand	401-402	2	31
β-strand	408	1	32
β-strand	412-417	6	32
β-strand	423	1	34
β-strand	431-432	2	31
β-strand	436-440	5	32
α-helix	453-455	3
β-strand	457	1	31
β-strand	464-467	4	32
α-helix	472-477	6
α-helix	484-486	3
β-strand	491	1	35
α-helix	496-498	3
β-strand	499	1	35

Chain C: 0 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	5-6	2	3
β-strand	19-24	6	3
β-strand	29-34	6	3
β-strand	38-39	2	36
β-strand	45-46	2	36

Chain D: 1 helix, 6 β-strands

Element	Residues	Length	Sheet
β-strand	5	1	37
β-strand	19-23	5	20
β-strand	24	1	37
β-strand	30-34	5	20
α-helix	35	1
β-strand	38-39	2	38
β-strand	45-46	2	38

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Epidermal Growth Factor Receptor	A, B	protein	501	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

>1MOX_1 Epidermal Growth Factor Receptor (chains A, B)
LEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYVQRNYDLSFLKTIQE
VAGYVLIALNTVERIPLENLQIIRGNMYYENSYALAVLSNYDANKTGLKELPMRNLQEIL
HGAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDFQNHLGSCQKCDPSCPNGSCWGAGE
ENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEATCKDTC
PPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEEDGVR
KCKKCEGPCRKVCNGIGIGEFKDSLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHT
PPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAFENLEIIRGRTKQHGQFSLAVVSLN
ITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKLFGTSGQKTKIISNRGENSCKATGQ
VCHALCSPEGCWGPEPRDCVS

Sequence of entity 2 (C, D), FASTA

>1MOX_2 Transforming Growth Factor alpha (chains C, D)
VVSHFNDCPDSHTQFCFHGTCRFLVQEDKPACVCHSGYVGARCEHADLLA

Ligands and cofactors

ID	Name	Formula	Copies
PT	Platinum (II) ion	Pt	7
CD	Cadmium ion	Cd	11
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	1

Water and common crystallization additives (CL) are not listed.

Primary citation

Crystal Structure of a Truncated Epidermal Growth Factor Receptor Extracellular Domain Bound to Transforming Growth Factor alpha. Garrett, T.P.J., McKern, N.M., Lou, M. et al. Cell (2002) 110:763-773. DOI 10.1016/S0092-8674(02)00940-6 · 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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