Structural basis for disfavored elimination reaction in catalytic antibody 1D4. Determined by X-ray diffraction at 1.8 Å resolution. Released 5 Dec 2001.
Explore 1JGU in 3D Show helices and sheets RCSB PDB PDBe
1JGU contains 19 α-helices and 45 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 | 7-8 | 2 | |
| β-strand | 10-12 | 3 | 8 |
| β-strand | 18-25 | 8 | 7 |
| β-strand | 32-39 | 8 | 8 |
| β-strand | 45-52 | 8 | 8 |
| β-strand | 56-59 | 4 | 8 |
| 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 | 8 |
| β-strand | 100B-103 | 4 | 8 |
| α-helix | 104-106 | 3 | |
| β-strand | 107-111 | 5 | 8 |
| β-strand | 117 | 1 | 9 |
| α-helix | 118-119 | 2 | |
| β-strand | 120-124 | 5 | 10 |
| α-helix | 125-127 | 3 | |
| β-strand | 135-145 | 11 | 10 |
| β-strand | 146 | 1 | 9 |
| β-strand | 151-154 | 4 | 11 |
| α-helix | 155-157 | 3 | |
| β-strand | 159 | 1 | 11 |
| β-strand | 163-165 | 3 | 10 |
| α-helix | 166-168 | 3 | |
| β-strand | 169-171 | 3 | 10 |
| β-strand | 174-184 | 11 | 10 |
| β-strand | 194-199 | 6 | 11 |
| α-helix | 200-202 | 3 | |
| β-strand | 204-209 | 6 | 11 |
| 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 | 122-126 | 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 |
| α-helix | 204 | 1 | |
| β-strand | 205-210 | 6 | 6 |
| α-helix | 211-213 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Antibody Light Chain | L | protein | 220 | Mus musculus | Q52L64 (AlphaFold model) |
| Antibody Heavy Chain | H | protein | 217 | Mus musculus | Q91Z05 (AlphaFold model) |
>1JGU_1 Antibody Light Chain (chains L) EVVMTQSPLSLPVSLGDQASISCRSSQSLVHSNGNTYLHWYLQKPGQSPKLLIYKVSNRF SGVPDRFSGSGSGTDFTLKISRVEAEDLGVYFCSQSTHVPPLTFGAGTKLELKRADAAPT VSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYS MSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>1JGU_2 Antibody Heavy Chain (chains H) EVKLVESRGGLVKPGGSLQLSCAASGFTFSGYAMSWFRLTPEKRLEWVASIYNGFRIHYL DSVKGRFTISSDYARNILYLQMSTLRSEDTAMYYCSRGDAYSRYFDVWGAGTTVTVSAAK TTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDLY TLSSSVTVTSSTWPSQSITCNVAHPASSTKVDKKIEP
| ID | Name | Formula | Copies |
|---|---|---|---|
| HBC | (2-amino-3-phenyl-BICYCLO[2.2.1]HEPT-2-yl)-phenyl-methanone | C20 H21 N O | 1 |
| OH | Hydroxide ion | H O | 1 |
Structural basis for a disfavored elimination reaction in catalytic antibody 1D4. Larsen, N.A., Heine, A., Crane, L. et al. J Mol Biol (2001) 314:93-102. DOI 10.1006/jmbi.2001.5112 · PubMed
Other PDB entries of the same protein (UniProt Q52L64 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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