Structure of IGG2A FAB fragment (D2.3) complexed with reaction product. Determined by X-ray diffraction at 2.0 Å resolution. Released 3 Dec 1997.
Explore 1YEG in 3D Show helices and sheets RCSB PDB PDBe
1YEG contains 15 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 | 34-39 | 6 | 8 |
| β-strand | 45-52 | 8 | 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 | 169-171 | 3 | 11 |
| α-helix | 172-174 | 3 | |
| β-strand | 175-177 | 3 | 11 |
| β-strand | 182-192 | 11 | 11 |
| β-strand | 203-210 | 7 | 12 |
| α-helix | 211-213 | 3 | |
| β-strand | 215-221 | 7 | 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 | 44-49 | 6 | 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 |
| β-strand | 114-118 | 5 | 5 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-126 | 5 | |
| 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 |
| β-strand | 205-210 | 6 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| IGG2A FAB fragment | L | protein | 219 | Mus musculus | |
| IGG2A FAB fragment | H | protein | 222 | Mus musculus | P01863 (AlphaFold model) |
>1YEG_1 IGG2A FAB FRAGMENT (chains L) DIVMTQSPLTLSVTIGQPASISCKSSQSLLYSNGKTYLNWLLQRPGQSPKRLIHLVSKLD SGVPDRITGSGSGTDFTLKISRVEAADLGVYYCVQGTHFPYTFGGGTKLEILRGDAAPTV SIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSM SSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>1YEG_2 IGG2A FAB FRAGMENT (chains H) EMQLQQSGAELLRPGTSVKLSCKTSGYIFTSYWIHWVKQRSGQGLEWIARIYPGTGSTYY NEKFKGKATLTADKSSSTAYMQLSTLKSEDSAVYFCTRWGFIPVREDYVMDYWGQGTLVT VSSAKTTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVL QSDLYTLSSSVTVTSSTWPSQSITCNVAHPASSTKVDKKIEP
Water and common crystallization additives (ACT) are not listed.
X-ray structures of a hydrolytic antibody and of complexes elucidate catalytic pathway from substrate binding and transition state stabilization through water attack and product release. Gigant, B., Charbonnier, J.B., Eshhar, Z. et al. Proc Natl Acad Sci U S A (1997) 94:7857-7861. DOI 10.1073/pnas.94.15.7857 · PubMed
Other PDB entries of the same protein (UniProt P01863 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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