Crystal structure of ErbB2 domains 1-3. Determined by X-ray diffraction at 2.5 Å resolution. Released 26 Jul 2005.
Explore 2A91 in 3D Show helices and sheets RCSB PDB PDBe
2A91 contains 20 α-helices and 50 β-strands across 1 chain. 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 | 4-6 | 3 | 1 |
| β-strand | 8 | 1 | 2 |
| α-helix | 13-15 | 3 | |
| α-helix | 18-29 | 12 | |
| β-strand | 34-36 | 3 | 1 |
| β-strand | 38 | 1 | 2 |
| β-strand | 39-42 | 4 | 3 |
| α-helix | 51-53 | 3 | |
| β-strand | 58-59 | 2 | 1 |
| β-strand | 63-66 | 4 | 3 |
| β-strand | 80-81 | 2 | 1 |
| β-strand | 87 | 1 | 3 |
| β-strand | 91-96 | 6 | 3 |
| β-strand | 118 | 1 | 4 |
| β-strand | 126-127 | 2 | 1 |
| β-strand | 131-135 | 5 | 3 |
| β-strand | 141 | 1 | 4 |
| α-helix | 148-151 | 4 | |
| β-strand | 152 | 1 | 1 |
| β-strand | 161-163 | 3 | 3 |
| α-helix | 170-175 | 6 | |
| β-strand | 183 | 1 | 5 |
| β-strand | 191 | 1 | 5 |
| α-helix | 192-194 | 3 | |
| β-strand | 206 | 1 | 6 |
| α-helix | 211-213 | 3 | |
| β-strand | 214 | 1 | 6 |
| α-helix | 215-216 | 2 | |
| β-strand | 219-223 | 5 | 7 |
| β-strand | 231-234 | 4 | 7 |
| β-strand | 237-239 | 3 | 8 |
| β-strand | 242-244 | 3 | 8 |
| α-helix | 247-249 | 3 | |
| β-strand | 251-253 | 3 | 9 |
| β-strand | 260-262 | 3 | 9 |
| β-strand | 268-270 | 3 | 8 |
| β-strand | 273-275 | 3 | 8 |
| α-helix | 278-279 | 2 | |
| β-strand | 283-284 | 2 | 10 |
| β-strand | 289 | 1 | 8 |
| β-strand | 290-291 | 2 | 10 |
| β-strand | 299-302 | 4 | 10 |
| β-strand | 308-311 | 4 | 10 |
| β-strand | 321-322 | 2 | 11 |
| β-strand | 324 | 1 | 12 |
| α-helix | 327-331 | 5 | |
| α-helix | 340-343 | 4 | |
| β-strand | 348-350 | 3 | 11 |
| β-strand | 352 | 1 | 12 |
| β-strand | 353-355 | 3 | 13 |
| α-helix | 357-361 | 5 | |
| β-strand | 363 | 1 | 14 |
| α-helix | 364-366 | 3 | |
| β-strand | 368 | 1 | 14 |
| α-helix | 369-372 | 4 | |
| α-helix | 375-381 | 7 | |
| β-strand | 384-385 | 2 | 11 |
| β-strand | 389-391 | 3 | 13 |
| α-helix | 402-404 | 3 | |
| β-strand | 409-410 | 2 | 11 |
| β-strand | 416 | 1 | 13 |
| β-strand | 420-425 | 6 | 13 |
| β-strand | 439-440 | 2 | 11 |
| β-strand | 444-448 | 5 | 13 |
| α-helix | 461-464 | 4 | |
| β-strand | 472-475 | 4 | 13 |
| α-helix | 480-485 | 6 | |
| β-strand | 499 | 1 | 15 |
| α-helix | 504-506 | 3 | |
| β-strand | 507 | 1 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Receptor tyrosine-protein kinase erbB-2 | A | protein | 517 | Homo sapiens | P04626 (AlphaFold model) |
>2A91_1 Receptor tyrosine-protein kinase erbB-2 (chains A) STQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNLELTYLPTNASLSFLQDIQEVQ GYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNGDPLNNTTPVTGASPGGLRELQ LRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQLALTLIDTNRSRACHPCSPMCKG SRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQCAAGCTGPKHSDCLACLHFNHS GICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTACPYNYLSTDVGSCTLVCPLHNQE VTAEDGTQKCEKCSKPCARVCYGLGMEHLREVRAVTSANIQEFAGCKKIFGSLAFLPESF DGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSLPDLSVFQNLQVIRGRILHNGAY SLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHTVPWDQLFRNPHQALLHTANRPE DECVGEGLACHQLCAKGHCWGPGPTQCVNDYKDDDDK
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 2 |
The Crystal Structure of a Truncated ErbB2 Ectodomain Reveals an Active Conformation, Poised to Interact with Other ErbB Receptors. Garrett, T.P.J., McKern, N.M., Lou, M. et al. Mol Cell (2003) 11:495-505. DOI 10.1016/S1097-2765(03)00048-0 · PubMed
Other PDB entries of the same protein (UniProt P04626 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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