crossreactive binding of a circularized peptide to an anti-TGFalpha antibody Fab-fragment. Determined by X-ray diffraction at 1.95 Å resolution. Released 12 Jul 2001.
Explore 1E4W in 3D Show helices and sheets RCSB PDB PDBe
1E4W contains 18 α-helices and 43 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 | 3-5 | 3 | 1 |
| β-strand | 9-12 | 4 | 2 |
| β-strand | 18-25 | 8 | 1 |
| β-strand | 33-39 | 7 | 2 |
| β-strand | 46-51 | 6 | 2 |
| β-strand | 57-59 | 3 | 2 |
| α-helix | 61-63 | 3 | |
| β-strand | 67-72 | 6 | 1 |
| α-helix | 73-75 | 3 | |
| β-strand | 77-82 | 6 | 1 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-95 | 8 | 2 |
| β-strand | 99-100 | 2 | 2 |
| β-strand | 104-108 | 5 | 2 |
| α-helix | 111-113 | 3 | |
| β-strand | 114 | 1 | 3 |
| α-helix | 115-116 | 2 | |
| β-strand | 117-121 | 5 | 4 |
| α-helix | 122-124 | 3 | |
| β-strand | 132-142 | 11 | 4 |
| β-strand | 143 | 1 | 3 |
| β-strand | 148-151 | 4 | 5 |
| α-helix | 152-154 | 3 | |
| β-strand | 156 | 1 | 5 |
| β-strand | 160-162 | 3 | 4 |
| α-helix | 163-165 | 3 | |
| β-strand | 166 | 1 | 4 |
| β-strand | 172-181 | 10 | 4 |
| β-strand | 191-196 | 6 | 5 |
| α-helix | 197-199 | 3 | |
| β-strand | 201-206 | 6 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 6 |
| β-strand | 10-13 | 4 | 7 |
| β-strand | 19-25 | 7 | 6 |
| β-strand | 33-38 | 6 | 7 |
| β-strand | 44-49 | 6 | 7 |
| β-strand | 53-54 | 2 | 7 |
| α-helix | 55 | 1 | |
| β-strand | 62-67 | 6 | 6 |
| β-strand | 70-75 | 6 | 6 |
| α-helix | 80-82 | 3 | |
| β-strand | 85-90 | 6 | 7 |
| α-helix | 96 | 1 | |
| β-strand | 97-98 | 2 | 7 |
| β-strand | 102-106 | 5 | 7 |
| β-strand | 111 | 1 | 8 |
| α-helix | 112-113 | 2 | |
| β-strand | 114-118 | 5 | 9 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-126 | 5 | |
| β-strand | 129-139 | 11 | 9 |
| β-strand | 140 | 1 | 8 |
| β-strand | 145-150 | 6 | 10 |
| β-strand | 153-155 | 3 | 10 |
| β-strand | 159-163 | 5 | 9 |
| α-helix | 164-167 | 4 | |
| β-strand | 173-182 | 10 | 9 |
| α-helix | 183-187 | 5 | |
| β-strand | 191-197 | 7 | 10 |
| α-helix | 204 | 1 | |
| β-strand | 205-210 | 6 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| TAB2 | H | protein | 213 | MUS MUSCULUS | P01865 (AlphaFold model) |
| TAB2 | L | protein | 214 | MUS MUSCULUS | P01837 (AlphaFold model) |
| Cyclic peptide | P | protein | 7 | synthetic construct |
>1E4W_1 TAB2 (chains H) QVQLQQPGAELVKPGASVKLSCKASGFTFTNYWMHWVKQRPGQGLEWIGEILPSNGRTNY NEKFKTKATLTVDKSSNTAYMQLSSLTSEDSAVYYCARSPSDYWGQGTTLTVSSAKTTAP SVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDLYTLSS SVTVTSSTWPSQSITCNVAHPASSTKVDKKIEP
>1E4W_2 TAB2 (chains L) DIQMTQTPSSLSASLGDRVTISCRASQDISHYLNWFQQKPDGTVKLLIYYTSTLHSGVPS RFSGSGSGTDYSLTISNLEEEDIAFYFCQQGGALPFTFGSGTKLAIKRADAAPTVSIFPP SSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLDSWTDQDSKDSTYSMSSTLT LTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>1E4W_3 CYCLIC PEPTIDE (chains P) SHFNEYE
| ID | Name | Formula | Copies |
|---|---|---|---|
| NI | Nickel (II) ion | Ni | 1 |
Water and common crystallization additives (CL) are not listed.
Cross-Reactive Binding of Cyclic Peptides to an Anti-Tgf Alpha Antibody Fab Fragment: An X-Ray Structural and Thermodynamic Analysis. Hahn, M., Winkler, D., Welfle, K. et al. J Mol Biol (2001) 314:293. DOI 10.1006/JMBI.2001.5135 · PubMed
Other PDB entries of the same protein (UniProt P01865 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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