Crystal structure of FAB198, an efficient protector of acetylcholine receptor against myasthenogenic antibodies. Determined by X-ray diffraction at 2.8 Å resolution. Released 26 Sept 2001.
Explore 1FN4 in 3D Show helices and sheets RCSB PDB PDBe
1FN4 contains 17 α-helices and 93 β-strands across 4 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 | 4-5 | 2 | 1 |
| β-strand | 10-12 | 3 | 2 |
| β-strand | 18-25 | 8 | 1 |
| β-strand | 33-37 | 5 | 2 |
| β-strand | 45-48 | 4 | 2 |
| β-strand | 66-67 | 2 | 1 |
| β-strand | 70-76 | 7 | 1 |
| β-strand | 85-90 | 6 | 2 |
| β-strand | 97 | 1 | 2 |
| β-strand | 102-105 | 4 | 2 |
| β-strand | 113 | 1 | 3 |
| α-helix | 119-122 | 4 | |
| β-strand | 123 | 1 | 4 |
| β-strand | 126-131 | 6 | 4 |
| β-strand | 132 | 1 | 3 |
| β-strand | 136 | 1 | 5 |
| β-strand | 144-145 | 2 | 6 |
| β-strand | 156-159 | 4 | 4 |
| α-helix | 162-164 | 3 | |
| β-strand | 170 | 1 | 5 |
| β-strand | 173-179 | 7 | 4 |
| β-strand | 188 | 1 | 7 |
| β-strand | 191-192 | 2 | 6 |
| β-strand | 203-204 | 2 | 6 |
| β-strand | 207 | 1 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-7 | 3 | 8 |
| β-strand | 11 | 1 | 9 |
| β-strand | 17-18 | 2 | 10 |
| β-strand | 21-23 | 3 | 8 |
| β-strand | 33-40 | 8 | 11 |
| β-strand | 46-51 | 6 | 11 |
| β-strand | 57-59 | 3 | 11 |
| α-helix | 61-64 | 4 | |
| β-strand | 67 | 1 | 10 |
| β-strand | 70-72 | 3 | 8 |
| α-helix | 73-75 | 3 | |
| β-strand | 77-79 | 3 | 8 |
| β-strand | 82-82A | 2 | 10 |
| β-strand | 88-95 | 8 | 11 |
| β-strand | 103 | 1 | 9 |
| β-strand | 113-117 | 5 | 12 |
| β-strand | 128 | 1 | 13 |
| β-strand | 131-136 | 6 | 12 |
| β-strand | 138 | 1 | 14 |
| α-helix | 148-150 | 3 | |
| β-strand | 156 | 1 | 12 |
| β-strand | 162-163 | 2 | 14 |
| β-strand | 168-169 | 2 | 14 |
| β-strand | 172-174 | 3 | 12 |
| β-strand | 177 | 1 | 13 |
| β-strand | 187 | 1 | 15 |
| β-strand | 192 | 1 | 16 |
| β-strand | 197 | 1 | 16 |
| β-strand | 202 | 1 | 15 |
| α-helix | 204-206 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-5 | 2 | 17 |
| β-strand | 10-12 | 3 | 18 |
| β-strand | 18-25 | 8 | 17 |
| β-strand | 33-37 | 5 | 18 |
| β-strand | 45-49 | 5 | 18 |
| β-strand | 53-54 | 2 | 18 |
| β-strand | 64-67 | 4 | 17 |
| β-strand | 70-76 | 7 | 17 |
| β-strand | 84-90 | 7 | 18 |
| β-strand | 97 | 1 | 18 |
| β-strand | 99 | 1 | 17 |
| β-strand | 102-105 | 4 | 18 |
| β-strand | 109 | 1 | 19 |
| β-strand | 112-115 | 4 | 20 |
| α-helix | 119-122 | 4 | |
| β-strand | 123 | 1 | 20 |
| β-strand | 126-136 | 11 | 20 |
| β-strand | 137 | 1 | 19 |
| β-strand | 144-147 | 4 | 21 |
| β-strand | 156-158 | 3 | 20 |
| α-helix | 162-164 | 3 | |
| β-strand | 170-179 | 10 | 20 |
| α-helix | 180-184 | 5 | |
| β-strand | 188 | 1 | 22 |
| β-strand | 189-192 | 4 | 21 |
| α-helix | 201-202 | 2 | |
| β-strand | 203-204 | 2 | 21 |
| β-strand | 207 | 1 | 22 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-7 | 5 | 23 |
| β-strand | 17-25 | 9 | 23 |
| β-strand | 33-38 | 6 | 24 |
| β-strand | 46-51 | 6 | 24 |
| β-strand | 57-59 | 3 | 24 |
| α-helix | 61-64 | 4 | |
| β-strand | 67-72 | 6 | 23 |
| α-helix | 73-75 | 3 | |
| β-strand | 77-82A | 7 | 23 |
| β-strand | 90-95 | 6 | 24 |
| β-strand | 110 | 1 | 25 |
| β-strand | 113-117 | 5 | 26 |
| β-strand | 128-138 | 11 | 26 |
| β-strand | 139 | 1 | 25 |
| α-helix | 148-150 | 3 | |
| β-strand | 157-158 | 2 | 26 |
| α-helix | 159-161 | 3 | |
| β-strand | 162-163 | 2 | 26 |
| β-strand | 168-170 | 3 | 26 |
| β-strand | 172-177 | 6 | 26 |
| α-helix | 178-181 | 4 | |
| β-strand | 187-189 | 3 | 27 |
| β-strand | 192 | 1 | 28 |
| α-helix | 193-195 | 3 | |
| β-strand | 197 | 1 | 28 |
| β-strand | 200-202 | 3 | 27 |
| α-helix | 204-206 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Monoclonal antibody against acetylcholine receptor | A, C | protein | 211 | Rattus norvegicus | P01835 (AlphaFold model) |
| Monoclonal antibody against acetylcholine receptor | B, D | protein | 218 | Rattus norvegicus | P20760 (AlphaFold model) |
>1FN4_1 MONOCLONAL ANTIBODY AGAINST ACETYLCHOLINE RECEPTOR (chains A, C) DIKLTQSPSLLSASVGDRVTLSCKGSQNINNYLAWYQQKLGEAPKLLIYNTNSLQTGIPS RFSGSGSGTDYTLTISSLQPEDVATYFCYQYNNGYTFGAGTKLELKRTAPTVSIFPPSTE QLATGGASVVCLMNNFYPRDISVKWKIDGTERRDGVLDSVTDQDSKDSTYSMSSTLSLTK ADYESHNLYTCEVVHKTSSSPVVKSFNRNEC
>1FN4_2 MONOCLONAL ANTIBODY AGAINST ACETYLCHOLINE RECEPTOR (chains B, D) QVQLLESGPGLVRPSETLSLTCTVSGFSLTSFSVSWVRHPSGKGPEWMGRMWYDGYTAYN SALKSRLSISRDTSKNQVFLKMNSLQTDDTGTYYCTRDLYGGYPLGFWYFDFWGPGTMVT VSSVFPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGALSSGVHTFPAVLQSGLYTL TSSVTVPSSTWSSQAVTCNVAHPASSTKVDKKIVPRDC
Crystal structure of Fab198, an efficient protector of the acetylcholine receptor against myasthenogenic antibodies. Poulas, K., Eliopoulos, E., Vatzaki, E. et al. Eur J Biochem (2001) 268:3685-3693. DOI 10.1046/j.1432-1327.2001.02274.x · PubMed
Other PDB entries of the same protein (UniProt P01835 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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