Cationic cyclization antibody 4C6 complex with transition state analog. Determined by X-ray diffraction at 2.45 Å resolution. Released 13 May 2003.
Explore 1ND0 in 3D Show helices and sheets RCSB PDB PDBe
1ND0 contains 54 α-helices and 181 β-strands across 8 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 | 4-7 | 4 | 1 |
| β-strand | 10-14 | 5 | 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 | 102-107 | 6 | 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 | 183-187 | 5 | |
| β-strand | 191-198 | 8 | 6 |
| β-strand | 201-210 | 10 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-7 | 5 | 7 |
| β-strand | 11-12 | 2 | 8 |
| β-strand | 18-25 | 8 | 7 |
| β-strand | 33-39 | 8 | 9 |
| β-strand | 45-52 | 8 | 9 |
| β-strand | 57-59 | 3 | 9 |
| α-helix | 61-63 | 3 | |
| β-strand | 67-72 | 6 | 7 |
| β-strand | 77-82 | 6 | 7 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-96 | 9 | 9 |
| β-strand | 102-103 | 2 | 9 |
| β-strand | 107-109 | 3 | 9 |
| β-strand | 110-111 | 2 | 8 |
| α-helix | 115-116 | 2 | |
| β-strand | 117 | 1 | 10 |
| β-strand | 120-124 | 5 | 11 |
| β-strand | 137-147 | 11 | 11 |
| β-strand | 148 | 1 | 10 |
| β-strand | 153-157 | 4 | 12 |
| α-helix | 162-164 | 3 | |
| β-strand | 171-173 | 3 | 11 |
| α-helix | 174-176 | 3 | |
| β-strand | 177-179 | 3 | 11 |
| β-strand | 184-194 | 11 | 11 |
| β-strand | 206-212 | 6 | 12 |
| α-helix | 213-215 | 3 | |
| β-strand | 217-222 | 6 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-7 | 5 | 31 |
| β-strand | 11-12 | 2 | 32 |
| β-strand | 18-25 | 8 | 31 |
| β-strand | 33-39 | 8 | 26 |
| β-strand | 45-52 | 8 | 26 |
| β-strand | 57-59 | 3 | 26 |
| α-helix | 61-63 | 3 | |
| β-strand | 67-68 | 2 | 31 |
| β-strand | 71-72 | 2 | 31 |
| β-strand | 77-82 | 6 | 31 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-96 | 9 | 26 |
| β-strand | 102-103 | 2 | 26 |
| β-strand | 107-109 | 3 | 26 |
| β-strand | 110-111 | 2 | 32 |
| α-helix | 115-116 | 2 | |
| β-strand | 117 | 1 | 33 |
| β-strand | 120-124 | 5 | 34 |
| β-strand | 137-147 | 11 | 34 |
| β-strand | 148 | 1 | 33 |
| β-strand | 153-157 | 4 | 35 |
| α-helix | 162-164 | 3 | |
| β-strand | 171-173 | 3 | 34 |
| α-helix | 174-176 | 3 | |
| β-strand | 177-179 | 3 | 34 |
| β-strand | 184-194 | 11 | 34 |
| β-strand | 206-212 | 6 | 35 |
| α-helix | 213-215 | 3 | |
| β-strand | 217-222 | 6 | 35 |
| α-helix | 226-227 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-7 | 5 | 42 |
| β-strand | 11-12 | 2 | 43 |
| β-strand | 18-25 | 8 | 42 |
| β-strand | 33-39 | 8 | 44 |
| β-strand | 45-52 | 8 | 44 |
| β-strand | 57-59 | 3 | 44 |
| α-helix | 61-63 | 3 | |
| β-strand | 67-72 | 6 | 42 |
| β-strand | 77-82 | 6 | 42 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-96 | 9 | 44 |
| β-strand | 102-103 | 2 | 44 |
| β-strand | 107-109 | 3 | 44 |
| β-strand | 110-111 | 2 | 43 |
| α-helix | 115-116 | 2 | |
| β-strand | 117 | 1 | 45 |
| β-strand | 120-124 | 5 | 46 |
| β-strand | 137-147 | 11 | 46 |
| β-strand | 148 | 1 | 45 |
| β-strand | 153-157 | 4 | 47 |
| α-helix | 162-164 | 3 | |
| β-strand | 171-173 | 3 | 46 |
| α-helix | 174-176 | 3 | |
| β-strand | 177-179 | 3 | 46 |
| β-strand | 184-194 | 11 | 46 |
| β-strand | 206-212 | 6 | 47 |
| α-helix | 213-215 | 3 | |
| β-strand | 217-222 | 6 | 47 |
| α-helix | 226-227 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Immunoglobulin IGG2A | A, C, E, G | protein | 219 | Mus musculus | Q58EU8 (AlphaFold model) |
| Immunoglobulin IGG2A | B, D, F, H | protein | 222 | Mus musculus | P01865 (AlphaFold model) |
>1ND0_1 IMMUNOGLOBULIN IGG2A (chains A, C, E, G) DVVMTQSPKTISVTIGQPASISCKSSQRLLNSNGKTFLNWLLQRPGQSPKRLIYLGTKLD SGVPDRFTGSGSGTDFTLKISRVEAEDLGVYYCWQGTHFPYTFGGGTKLEIKRADAAPTV SIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSM SSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>1ND0_2 IMMUNOGLOBULIN IGG2A (chains B, D, F, H) RVQLQQSGPGLVKPSQSLSLTCTVTGYSITSDFAWNWIRQFPGNKLEWMGYINYSGFTSH NPSLKSRISITRDTSKNQFFLQLNSVTTEDTATYYCAGLLWYDGGAGSWGQGTLVTVSAA KTTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDL YTLSSSVTVTSSTWPSQSITCNVAHPASSTKVDKKIEPRGPT
| ID | Name | Formula | Copies |
|---|---|---|---|
| DP4 | (1s,4s)-4-[dimethyl(phenyl)silyl]-1-methylpiperidine 1-oxide | C14 H23 N O Si | 4 |
Water and common crystallization additives (SO4) are not listed.
Structural Basis for Antibody Catalysis of a Cationic Cyclization Reaction. Zhu, X., Heine, A., Monnat, F. et al. J Mol Biol (2003) 329:69-83. DOI 10.1016/S0022-2836(03)00406-6 · PubMed
Other PDB entries of the same protein (UniProt Q58EU8 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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