Immune versus natural selection: antibody aldolases with the rates of natural enzymes. Determined by X-ray diffraction at 2.15 Å resolution. Released 28 Oct 1998.
Explore 1AXT in 3D Show helices and sheets RCSB PDB PDBe
1AXT contains 13 α-helices and 44 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 | 10-12 | 3 | 8 |
| β-strand | 18-25 | 8 | 7 |
| α-helix | 29-31 | 3 | |
| β-strand | 33-40 | 8 | 8 |
| β-strand | 44-51 | 8 | 8 |
| α-helix | 52B-53 | 3 | |
| β-strand | 57-59 | 3 | 8 |
| 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 | 99-103 | 4 | 8 |
| β-strand | 107-111 | 5 | 8 |
| α-helix | 114-116 | 3 | |
| β-strand | 117 | 1 | 9 |
| α-helix | 118-119 | 2 | |
| β-strand | 120-124 | 5 | 10 |
| β-strand | 137-147 | 11 | 10 |
| β-strand | 148 | 1 | 9 |
| β-strand | 153-157 | 4 | 11 |
| α-helix | 162-164 | 3 | |
| β-strand | 166 | 1 | 11 |
| β-strand | 171-179 | 9 | 10 |
| β-strand | 184-194 | 11 | 10 |
| β-strand | 206-212 | 6 | 11 |
| α-helix | 213-215 | 3 | |
| β-strand | 217-222 | 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-27E | 3 | 3 |
| β-strand | 30-31 | 2 | 3 |
| β-strand | 33-38 | 6 | 2 |
| β-strand | 44-49 | 6 | 2 |
| β-strand | 53-54 | 2 | 2 |
| 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 |
| 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 | 153-154 | 2 | 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 | 191-197 | 7 | 6 |
| β-strand | 205-210 | 6 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Immunoglobulin IGG2A | L | protein | 216 | Mus musculus | |
| Immunoglobulin IGG2A | H | protein | 218 | Mus musculus | P01865 (AlphaFold model) |
>1AXT_1 IMMUNOGLOBULIN IGG2A (chains L) ELVMTQTPLSLPVSLGDQASISCRSSQSLVHSYGNTFLNWYLQKSGQSPKLLIYKVSNRF SGVPDRFSGSGSGTDFTLKISRVEAEDLGVYFCSQGTHVPYTFGGGTKLEIKRADAAPTV SIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSM SSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNR
>1AXT_2 IMMUNOGLOBULIN IGG2A (chains H) EVKLEESGGGLVQPGGSMKLSCVVSGLTFSRFWMSWVRQSPEKGLEWVAEIRLKSDNYAT HYAESVKGKFTISRDDSKSRLYLQMNSLRTEDTGIYYCKIYFYSFSYWGQGTLVTVSAAK TTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDLY TLSSSVTVTSSTWPSQSITCNVAHPASSTKVDKKIEPR
Immune versus natural selection: antibody aldolases with enzymic rates but broader scope. Barbas 3rd., C.F., Heine, A., Zhong, G. et al. Science (1997) 278:2085-2092. DOI 10.1126/science.278.5346.2085 · PubMed
Other PDB entries of the same protein (UniProt P01865 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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