Structure of the extracellular domain of human epidermal growth factor (EGF) receptor in an inactive (low pH) complex with EGF. Determined by X-ray diffraction at 2.8 Å resolution. Released 11 Mar 2003.
Explore 1NQL in 3D Show helices and sheets RCSB PDB PDBe
1NQL contains 23 α-helices and 80 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6-7 | 2 | 1 |
| β-strand | 16-17 | 2 | 2 |
| α-helix | 20-31 | 12 | |
| β-strand | 36-37 | 2 | 1 |
| β-strand | 41-44 | 4 | 3 |
| α-helix | 54-57 | 4 | |
| β-strand | 60-61 | 2 | 1 |
| β-strand | 65-68 | 4 | 3 |
| β-strand | 74 | 1 | 4 |
| β-strand | 82-83 | 2 | 1 |
| β-strand | 89 | 1 | 3 |
| β-strand | 93-98 | 6 | 3 |
| β-strand | 110 | 1 | 4 |
| β-strand | 118-119 | 2 | 1 |
| β-strand | 123-127 | 5 | 3 |
| α-helix | 135-137 | 3 | |
| α-helix | 140-143 | 4 | |
| β-strand | 144 | 1 | 1 |
| α-helix | 146-151 | 6 | |
| β-strand | 153-154 | 2 | 3 |
| α-helix | 164-167 | 4 | |
| α-helix | 171-173 | 3 | |
| β-strand | 175 | 1 | 5 |
| α-helix | 180-182 | 3 | |
| β-strand | 183 | 1 | 5 |
| β-strand | 199 | 1 | 6 |
| α-helix | 204-206 | 3 | |
| β-strand | 207 | 1 | 6 |
| α-helix | 208-209 | 2 | |
| β-strand | 212 | 1 | 7 |
| β-strand | 216 | 1 | 8 |
| β-strand | 224 | 1 | 8 |
| β-strand | 227 | 1 | 7 |
| β-strand | 230-232 | 3 | 9 |
| β-strand | 235-237 | 3 | 9 |
| β-strand | 244-247 | 4 | 10 |
| β-strand | 252-255 | 4 | 10 |
| β-strand | 261-263 | 3 | 9 |
| β-strand | 266-268 | 3 | 9 |
| β-strand | 276-277 | 2 | 11 |
| β-strand | 283-284 | 2 | 11 |
| β-strand | 291 | 1 | 12 |
| β-strand | 295 | 1 | 13 |
| β-strand | 300 | 1 | 13 |
| β-strand | 301 | 1 | 11 |
| β-strand | 304 | 1 | 12 |
| β-strand | 312-313 | 2 | 14 |
| β-strand | 317 | 1 | 15 |
| α-helix | 319-321 | 3 | |
| β-strand | 322 | 1 | 15 |
| α-helix | 332-335 | 4 | |
| β-strand | 340-341 | 2 | 14 |
| β-strand | 345-347 | 3 | 16 |
| α-helix | 350-353 | 4 | |
| β-strand | 355 | 1 | 17 |
| β-strand | 360 | 1 | 17 |
| α-helix | 361-364 | 4 | |
| α-helix | 365-373 | 9 | |
| β-strand | 376-377 | 2 | 14 |
| β-strand | 381-383 | 3 | 16 |
| β-strand | 392 | 1 | 18 |
| α-helix | 394-396 | 3 | |
| β-strand | 401-402 | 2 | 14 |
| β-strand | 408 | 1 | 16 |
| β-strand | 412-417 | 6 | 16 |
| β-strand | 423 | 1 | 18 |
| β-strand | 431-432 | 2 | 14 |
| β-strand | 436-440 | 5 | 16 |
| α-helix | 453-455 | 3 | |
| β-strand | 457 | 1 | 14 |
| β-strand | 466-467 | 2 | 16 |
| α-helix | 472-478 | 7 | |
| β-strand | 486 | 1 | 19 |
| β-strand | 491 | 1 | 20 |
| α-helix | 496-498 | 3 | |
| β-strand | 499 | 1 | 20 |
| β-strand | 502 | 1 | 19 |
| β-strand | 505-507 | 3 | 21 |
| β-strand | 510-512 | 3 | 21 |
| β-strand | 524-526 | 3 | 22 |
| β-strand | 530 | 1 | 21 |
| β-strand | 531-533 | 3 | 22 |
| α-helix | 534-535 | 2 | |
| β-strand | 538 | 1 | 23 |
| α-helix | 539-540 | 2 | |
| β-strand | 547 | 1 | 24 |
| β-strand | 555 | 1 | 24 |
| β-strand | 558 | 1 | 23 |
| β-strand | 561-563 | 3 | 25 |
| β-strand | 566-568 | 3 | 25 |
| β-strand | 573-576 | 4 | 26 |
| β-strand | 582-584 | 3 | 26 |
| β-strand | 585-587 | 3 | 27 |
| β-strand | 592 | 1 | 25 |
| β-strand | 593-595 | 3 | 27 |
| α-helix | 596-597 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-5 | 2 | 28 |
| β-strand | 13-14 | 2 | 28 |
| β-strand | 19-23 | 5 | 2 |
| β-strand | 28-33 | 6 | 2 |
| α-helix | 34 | 1 | |
| β-strand | 37-38 | 2 | 29 |
| β-strand | 44-45 | 2 | 29 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| epidermal growth factor receptor | A | protein | 624 | Homo sapiens | P00533 (AlphaFold model) |
| epidermal growth factor | B | protein | 53 | Homo sapiens | P01133 (AlphaFold model) |
>1NQL_1 epidermal growth factor receptor (chains A) LEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYVQRNYDLSFLKTIQE VAGYVLIALNTVERIPLENLQIIRGNMYYENSYALAVLSNYDANKTGLKELPMRNLQEIL HGAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDFQNHLGSCQKCDPSCPNGSCWGAGE ENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEATCKDTC PPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEEDGVR KCKKCEGPCRKVCNGIGIGEFKDSLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHT PPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAFENLEIIRGRTKQHGQFSLAVVSLN ITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKLFGTSGQKTKIISNRGENSCKATGQ VCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCKLLEGEPREFVENSECIQCHPECLP QAMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNC TYGCTGPGLEGCPTNGPKHHHHHH
>1NQL_2 epidermal growth factor (chains B) NSDSECPLSHDGYCLHDGVCMYIEALDKYACNCVVGYIGERCQYRDLKWWELR
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 5 |
EGF activates its receptor by removing interactions that auto-inhibit ectodomain dimerization. Ferguson, K.M., Berger, M.B., Mendrola, J.M. et al. Mol Cell (2003) 11:507-517. DOI 10.1016/S1097-2765(03)00047-9 · PubMed
Other PDB entries of the same protein (UniProt P00533 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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