Structure of a catalytic antibody, IGG2A FAB fragment (D2.5). Determined by X-ray diffraction at 2.2 Å resolution. Released 15 Oct 1997.
Explore 1YEE in 3D Show helices and sheets RCSB PDB PDBe
1YEE contains 16 α-helices and 47 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 | 3-6 | 4 | 7 |
| α-helix | 7-9 | 3 | |
| β-strand | 10-12 | 3 | 8 |
| β-strand | 18-25 | 8 | 7 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-40 | 7 | 8 |
| β-strand | 44-52 | 9 | 8 |
| β-strand | 56-59 | 4 | 8 |
| α-helix | 61-63 | 3 | |
| β-strand | 64 | 1 | 7 |
| β-strand | 67-72 | 6 | 7 |
| β-strand | 77-82 | 6 | 7 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-94 | 7 | 8 |
| β-strand | 97-98 | 2 | 9 |
| β-strand | 100C-100D | 2 | 9 |
| β-strand | 102-103 | 2 | 8 |
| β-strand | 107-111 | 5 | 8 |
| α-helix | 114-116 | 3 | |
| β-strand | 117 | 1 | 10 |
| β-strand | 120-124 | 5 | 11 |
| β-strand | 135-145 | 11 | 11 |
| β-strand | 146 | 1 | 10 |
| β-strand | 151-155 | 4 | 12 |
| α-helix | 160-162 | 3 | |
| β-strand | 164 | 1 | 12 |
| β-strand | 169-177 | 9 | 11 |
| β-strand | 182-192 | 11 | 11 |
| β-strand | 204-210 | 6 | 12 |
| α-helix | 211-213 | 3 | |
| β-strand | 215-220 | 6 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 1 |
| β-strand | 10-13 | 4 | 2 |
| β-strand | 19-25 | 7 | 1 |
| β-strand | 27C | 1 | 3 |
| β-strand | 31 | 1 | 3 |
| β-strand | 33-38 | 6 | 2 |
| β-strand | 45-49 | 5 | 2 |
| β-strand | 53-54 | 2 | 2 |
| α-helix | 55 | 1 | |
| β-strand | 62-67 | 6 | 1 |
| β-strand | 70-75 | 6 | 1 |
| α-helix | 80-82 | 3 | |
| β-strand | 84-90 | 7 | 2 |
| α-helix | 96 | 1 | |
| β-strand | 97-98 | 2 | 2 |
| β-strand | 102-106 | 5 | 2 |
| β-strand | 111 | 1 | 4 |
| α-helix | 112-113 | 2 | |
| β-strand | 114-118 | 5 | 5 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-125 | 4 | |
| β-strand | 129-139 | 11 | 5 |
| β-strand | 140 | 1 | 4 |
| β-strand | 145-150 | 6 | 6 |
| β-strand | 153-155 | 3 | 6 |
| β-strand | 159-163 | 5 | 5 |
| α-helix | 164-167 | 4 | |
| β-strand | 173-182 | 10 | 5 |
| α-helix | 183-186 | 4 | |
| β-strand | 191-197 | 7 | 6 |
| α-helix | 204 | 1 | |
| β-strand | 205-210 | 6 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| IGG2A FAB fragment (D2.5) | L | protein | 219 | Mus musculus | |
| IGG2A FAB fragment (D2.5) | H | protein | 222 | Mus musculus | P01865 (AlphaFold model) |
>1YEE_1 IGG2A FAB FRAGMENT (D2.5) (chains L) DIVMTQSPLTLSVTIGQPASISCKSSQSLLYSNGKTYLSWLLQRPGQSPKRLIYLVSKLD SGVPDRFTGSGSGTDFTLKISRVEAADLGLYYCVQGTHFPYTFGGGTKLEILRADAAPTV SIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSM SSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>1YEE_2 IGG2A FAB FRAGMENT (D2.5) (chains H) EVKLQESGAELVRPGASVKLSCKTSGYIFTSYWIHWVKQRAAAGLEWIARIYPGTGSSYY NVKFKGKATLTADKSSSTAYMQLSSLKSDDSAVYFCVRWGFIPVREDYVLDYWGQGTLVT VSSAKTTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVL QSDLYTLSSSVTVTSSTWPSQSITCNVAHPASSTKVDKKIEP
| ID | Name | Formula | Copies |
|---|---|---|---|
| PNB | 4-nitro-benzylphosphonobutanoyl-glycine | C13 H17 N2 O8 P | 1 |
Structural convergence in the active sites of a family of catalytic antibodies. Charbonnier, J.B., Golinelli-Pimpaneau, B., Gigant, B. et al. Science (1997) 275:1140-1142. DOI 10.1126/science.275.5303.1140 · 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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