Thermodynamic and structural analyses of hydrolytic mechanism by catalytic antibodies. Determined by X-ray diffraction at 2.25 Å resolution. Released 29 May 2007.
Explore 2DTM in 3D Show helices and sheets RCSB PDB PDBe
2DTM contains 17 α-helices and 46 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 | 3-7 | 5 | 7 |
| β-strand | 11-12 | 2 | 8 |
| β-strand | 18-25 | 8 | 7 |
| α-helix | 29-31 | 3 | |
| β-strand | 33-39 | 7 | 9 |
| β-strand | 45-51 | 7 | 9 |
| β-strand | 57-59 | 3 | 9 |
| 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 | 88-97 | 10 | 9 |
| β-strand | 100I-103 | 6 | 9 |
| β-strand | 107-109 | 3 | 9 |
| β-strand | 110-111 | 2 | 8 |
| α-helix | 115-116 | 2 | |
| β-strand | 117 | 1 | 10 |
| α-helix | 118-119 | 2 | |
| β-strand | 120-124 | 5 | 11 |
| β-strand | 135-145 | 11 | 11 |
| β-strand | 146 | 1 | 10 |
| β-strand | 151-154 | 4 | 12 |
| α-helix | 155-157 | 3 | |
| β-strand | 163-165 | 3 | 11 |
| α-helix | 166-168 | 3 | |
| β-strand | 169-171 | 3 | 11 |
| β-strand | 174-184 | 11 | 11 |
| α-helix | 185-187 | 3 | |
| β-strand | 194-199 | 6 | 12 |
| α-helix | 200-202 | 3 | |
| β-strand | 204-209 | 6 | 12 |
| α-helix | 211-213 | 3 |
| 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 | 122-125 | 4 | |
| 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 |
| 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 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Immunoglobulin 6D9 | L | protein | 219 | Mus musculus | A2NHM3 (AlphaFold model) |
| Immunoglobulin 6D9 | H | protein | 224 | Mus musculus | P18527 (AlphaFold model) |
>2DTM_1 IMMUNOGLOBULIN 6D9 (chains L) DVLMTQTPLSLPVSLGDQASISCRSSQTIVHSNGDTYLDWFLQKPGQSPKLLIYKVSNRF SGVPDRFSGSGSGTDFTLKISRVEAEDLGVYYCFQGSHVPPTFGGGTKLEIKRADAAPTV SIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSM SSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>2DTM_2 IMMUNOGLOBULIN 6D9 (chains H) EVKLVESGGGLVKPGGSLKLSCAASGFTFSNYAMSWVRQTPEKRLEWVVSISSGGSIYYL DSVKGRFTVSRDNARNILYLQMTSLRSEDTAMYFCARVSHYDGSRDWYFDVWGAGTSVTV SSAKTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQ SDLYTLSSSVTVPSSTWPSETVTCNVAHPASSTKVDKKIVPRDC
Thermodynamic and structural basis for transition-state stabilization in antibody-catalyzed hydrolysis. Oda, M., Ito, N., Tsumuraya, T. et al. J Mol Biol (2007) 369:198-209. DOI 10.1016/j.jmb.2007.03.023 · PubMed
Other PDB entries of the same protein (UniProt A2NHM3 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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