N1G9 (IgG1-lambda) FAB fragment. Determined by X-ray diffraction at 2.4 Å resolution. Released 11 Jul 1996.
Explore 1NGQ in 3D Show helices and sheets RCSB PDB PDBe
1NGQ contains 9 α-helices and 48 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 | 7 |
| β-strand | 9-12 | 4 | 8 |
| β-strand | 18-25 | 8 | 7 |
| α-helix | 29-31 | 3 | |
| β-strand | 33-39 | 7 | 8 |
| β-strand | 41 | 1 | 9 |
| β-strand | 43 | 1 | 9 |
| β-strand | 45-51 | 7 | 8 |
| β-strand | 58-60 | 3 | 8 |
| β-strand | 68-73 | 6 | 7 |
| β-strand | 78-83 | 6 | 7 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-99 | 8 | 8 |
| β-strand | 109 | 1 | 2 |
| β-strand | 110 | 1 | 8 |
| β-strand | 114-118 | 5 | 8 |
| β-strand | 124 | 1 | 10 |
| β-strand | 127-131 | 5 | 11 |
| β-strand | 142-152 | 11 | 11 |
| β-strand | 153 | 1 | 10 |
| β-strand | 158-161 | 4 | 12 |
| α-helix | 162-164 | 3 | |
| β-strand | 166 | 1 | 12 |
| β-strand | 170-172 | 3 | 11 |
| α-helix | 173-175 | 3 | |
| β-strand | 176-177 | 2 | 11 |
| β-strand | 182-191 | 10 | 11 |
| β-strand | 200-206 | 7 | 12 |
| β-strand | 211-217 | 7 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-6 | 3 | 1 |
| β-strand | 9-12 | 4 | 2 |
| β-strand | 17-24 | 8 | 1 |
| α-helix | 31-33 | 3 | |
| β-strand | 36-41 | 6 | 2 |
| β-strand | 45-51 | 7 | 2 |
| β-strand | 55-56 | 2 | 2 |
| α-helix | 57 | 1 | |
| β-strand | 64-69 | 6 | 1 |
| β-strand | 72-78 | 7 | 1 |
| α-helix | 82-84 | 3 | |
| β-strand | 86-93 | 8 | 2 |
| β-strand | 98-100 | 3 | 2 |
| β-strand | 104-108 | 5 | 2 |
| β-strand | 114 | 1 | 3 |
| β-strand | 117-121 | 5 | 4 |
| α-helix | 122-124 | 3 | |
| β-strand | 132-142 | 11 | 4 |
| β-strand | 143 | 1 | 3 |
| β-strand | 147-151 | 5 | 5 |
| β-strand | 152-153 | 2 | 6 |
| β-strand | 156-157 | 2 | 6 |
| β-strand | 162-164 | 3 | 4 |
| β-strand | 168-169 | 2 | 4 |
| β-strand | 175-184 | 10 | 4 |
| α-helix | 185-190 | 6 | |
| β-strand | 193-200 | 8 | 5 |
| β-strand | 203-210 | 8 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| N1G9 (IgG1-lambda) | L | protein | 215 | Mus musculus | G0YP42 (AlphaFold model) |
| N1G9 (IgG1-lambda) | H | protein | 222 | Mus musculus | P01751 |
>1NGQ_1 N1G9 (IGG1-LAMBDA) (chains L) QAVVTQESALTTSPGETVTLTCRSSTGAVTTSNYANWVQEKPDHLFTGLIGGTNNRAPGV PARFSGSLIGDKAALTITGAQTEDEAIYFCALWYSNHWVFGGGTKLTVLGQPKSSPSVTL FPPSSEELETNKATLVCTITDFYPGVVTVDWKVDGTPVTQGMETTQPSKQSNNKYMASSY LTLTARAWERHSSYSCQVTHEGHTVEKSLSRADCS
>1NGQ_2 N1G9 (IGG1-LAMBDA) (chains H) QVQLQQPGAELVKPGASVKLSCKASGYTFTSYWMHWVKQRPGRGLEWIGRIDPNSGGTKY NEKFKSKATLTVDKPSSTAYMQLSSLTSEDSAVYYCARYDYYGSSYFDYWGQGTTLTVSS AKTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSD LYTLSSSVTVPSSPWPSETVTCNVAHPASSTKVDKKIVPRDC
Three-dimensional structures of the Fab fragment of murine N1G9 antibody from the primary immune response and of its complex with (4-hydroxy-3-nitrophenyl)acetate. Mizutani, R., Miura, K., Nakayama, T. et al. J Mol Biol (1995) 254:208-222. DOI 10.1006/jmbi.1995.0612 · PubMed
Other PDB entries of the same protein (UniProt G0YP42 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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