4UIP: Epidermal growth factor receptor

The complex structure of extracellular domain of EGFR with Repebody (rAC1). Determined by X-ray diffraction at 2.95 Å resolution. Released 25 Nov 2015.

Method
X-ray diffraction
Resolution
2.95 Å
Organisms
HOMO SAPIENS, LISTERIA MONOCYTOGENES, SYNTHETIC CONSTRUCT
Chains
2
Atoms
6,680
Mol. weight
97.76 kDa
Ligands
NAG
Released
25 Nov 2015

Explore 4UIP in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4UIP contains 30 α-helices and 83 β-strands across 2 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: 20 helices, 68 β-strands

ElementResiduesLengthSheet
β-strand6-721
β-strand1012
α-helix20-3011
β-strand36-3721
β-strand4012
β-strand41-4443
α-helix53-575
β-strand60-6121
β-strand65-6843
β-strand7414
β-strand82-8321
β-strand93-9863
β-strand10115
β-strand10715
β-strand11014
β-strand118-11921
β-strand123-12753
β-strand14411
α-helix149-1513
β-strand153-15423
α-helix171-1733
β-strand17516
α-helix180-1823
β-strand18316
α-helix184-1852
β-strand19917
β-strand20717
β-strand21218
β-strand21619
β-strand22419
β-strand22718
β-strand230-231210
β-strand236-237210
α-helix240-2423
β-strand244-246311
β-strand253-255311
β-strand261-263310
β-strand266-268310
β-strand276-277212
β-strand282110
β-strand283-284212
β-strand291-296612
β-strand299-304612
α-helix309-3102
β-strand312-314313
α-helix319-3213
α-helix333-3353
β-strand340-342313
β-strand345-347314
α-helix350-3534
β-strand355115
β-strand360115
α-helix361-3633
α-helix365-3739
β-strand376-377213
β-strand381-383314
β-strand401-402213
β-strand408114
β-strand412-417614
β-strand431-432213
β-strand436-440514
α-helix448-4503
α-helix453-4564
β-strand457113
β-strand464-467414
α-helix472-4776
β-strand486116
β-strand491117
β-strand499117
β-strand502116
β-strand506118
β-strand524-527418
β-strand530-533418
α-helix534-5352
β-strand538119
α-helix539-5413
β-strand547120
β-strand555120
β-strand558119
β-strand561-563321
β-strand566-568321
β-strand573-576422
α-helix578-5803
β-strand582-584322
β-strand585-587323
β-strand592121
β-strand593-595323
α-helix596-5972
Chain B: 10 helices, 15 β-strands
ElementResiduesLengthSheet
β-strand8-9224
α-helix10-134
α-helix17-2610
β-strand35-36224
α-helix38-414
β-strand46-48325
α-helix60-623
β-strand68-70325
α-helix80-823
β-strand90-92325
α-helix101-1022
β-strand114-116325
β-strand138-140325
α-helix149-1502
β-strand162-164325
β-strand186-188325
β-strand194126
α-helix202-2109
β-strand215-216225
β-strand222125
α-helix224-2263
β-strand228127
β-strand229126
β-strand235127
α-helix236-2383

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Epidermal growth factor receptorAprotein618HOMO SAPIENSP00533 (AlphaFold model)
Repebody (RAC1)Bprotein251LISTERIA MONOCYTOGENES, SYNTHETIC CONSTRUCT, EPTATRETUS BURGERIE0ACT6 (AlphaFold model), Q4G1L3 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4UIP_1 EPIDERMAL GROWTH FACTOR RECEPTOR (chains A)
EEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYVQRNYDLSFLKTIQEV
AGYVLIALNTVERIPLENLQIIRGNMYYENSYALAVLSNYDANKTGLKELPMRNLQEILH
GAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDFQNHLGSCQKCDPSCPNGSCWGAGEE
NCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEATCKDTCP
PLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEEDGVRK
CKKCEGPCRKVCNGIGIGEFKDSLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHTP
PLDPQELDILKTVKEITGFLLIQAWPENRTDLHAFENLEIIRGRTKQHGQFSLAVVSLNI
TSLGLRSLKEISDGDVIISGNKNLCYANTINWKKLFGTSGQKTKIISNRGENSCKATGQV
CHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCNLLEGEPREFVENSECIQCHPECLPQ
AMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNCT
YGCTGPGLEGCPHHHHHH
Sequence of entity 2 (B), FASTA
>4UIP_2 REPEBODY (RAC1) (chains B)
METITVSTPIKQIFPDDAFAETIKANLKKKSVTDAVTQNELNSIDQIIANNSDIKSVQGI
QYLPNVRYLALGGNKLHDISALKELTNLTYLMLHYNQLQILPNGVFDKLTNLKELYLSEN
QLQSLPDGVFDKLTNLTELDLARNQLQSLPKGVFDKLTQLKDLRLYQNQLKSVPDGVFDR
LTSLQYIWLHDNPWDCTCPGIRYLSEWINKHSGVVRNSAGSVAPDSAKCSGSGKPVRSII
CPTLEHHHHHH

Ligands and cofactors

IDNameFormulaCopies
NAG2-acetamido-2-deoxy-beta-D-glucopyranoseC8 H15 N O62

Primary citation

Enzymatic Prenylation and Oxime Ligation for the Synthesis of Stable and Homogeneous Protein-Drug Conjugates for Targeted Therapy. Lee, J., Choi, H., Yun, M. et al. Angew Chem Int Ed Engl (2015) 54:12020. DOI 10.1002/ANIE.201505964 · PubMed

Other PDB entries of the same protein (UniProt P00533 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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