29G11 complexed with phenyl [1-(1-N-succinylamino)pentyl] phosphonate. Determined by X-ray diffraction at 2.3 Å resolution. Released 2 Mar 1999.
Explore 1A0Q in 3D Show helices and sheets RCSB PDB PDBe
1A0Q contains 16 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 | 3-6 | 4 | 6 |
| α-helix | 7-9 | 3 | |
| β-strand | 10-12 | 3 | 7 |
| β-strand | 18-25 | 8 | 6 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 7 |
| β-strand | 45-51 | 7 | 7 |
| β-strand | 57-59 | 3 | 7 |
| α-helix | 61-63 | 3 | |
| β-strand | 64 | 1 | 6 |
| β-strand | 67-72 | 6 | 6 |
| α-helix | 73-75 | 3 | |
| β-strand | 77-82 | 6 | 6 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-94 | 7 | 7 |
| β-strand | 103 | 1 | 7 |
| β-strand | 107-111 | 5 | 7 |
| α-helix | 114-116 | 3 | |
| β-strand | 117 | 1 | 8 |
| β-strand | 120-124 | 5 | 9 |
| β-strand | 135-145 | 11 | 9 |
| β-strand | 146 | 1 | 8 |
| β-strand | 151-154 | 4 | 10 |
| α-helix | 155-157 | 3 | |
| β-strand | 159 | 1 | 10 |
| β-strand | 163-165 | 3 | 9 |
| α-helix | 166-168 | 3 | |
| β-strand | 169-171 | 3 | 9 |
| β-strand | 174-184 | 11 | 9 |
| α-helix | 185-187 | 3 | |
| β-strand | 194-199 | 6 | 10 |
| α-helix | 200-202 | 3 | |
| β-strand | 204-209 | 6 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 1 |
| β-strand | 10-13 | 4 | 2 |
| β-strand | 19-25 | 7 | 1 |
| β-strand | 33-38 | 6 | 2 |
| β-strand | 44-49 | 6 | 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 | 85-90 | 6 | 2 |
| β-strand | 97-98 | 2 | 2 |
| β-strand | 102-106 | 5 | 2 |
| β-strand | 111 | 1 | 3 |
| β-strand | 114-118 | 5 | 4 |
| α-helix | 119-121 | 3 | |
| α-helix | 124-126 | 3 | |
| β-strand | 129-139 | 11 | 4 |
| β-strand | 140 | 1 | 3 |
| β-strand | 145-150 | 6 | 5 |
| β-strand | 153-155 | 3 | 5 |
| β-strand | 159-163 | 5 | 4 |
| α-helix | 164-167 | 4 | |
| β-strand | 173-182 | 10 | 4 |
| α-helix | 183-187 | 5 | |
| β-strand | 191-197 | 7 | 5 |
| β-strand | 205-210 | 6 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 29G11 FAB (light chain) | L | protein | 212 | Mus musculus | P01837 (AlphaFold model) |
| 29G11 FAB (heavy chain) | H | protein | 217 | Mus musculus | P01869 (AlphaFold model) |
>1A0Q_1 29G11 FAB (LIGHT CHAIN) (chains L) DIELTQSPSSLSASLGGKVTITCKASQDIKKYIGWYQHKPGKQPRLLIHYTSTLLPGIPS RFRGSGSGRDYSFSISNLEPEDIATYYCLQYYNLRTFGGGTKLEIKRADAAPTVSIFPPS SEQLTSGGASVVCFLNNFYSKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTL TKDEYERHNSYTCEATHKTSTSPIVKSFNRNE
>1A0Q_2 29G11 FAB (HEAVY CHAIN) (chains H) EVQLQESDAELVKPGASVKISCKASGYTFTDHVIHWVKQKPEQGLEWIGYISPGNGDIKY NEKFKGKATLTADKSSSTAYMQLNSLTSEDSAVYLCKRGYYGRSNVDYWGQGTTLTVSSA KTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDL YTLSSSVTVPSSTWPSETVTCNVAHPASSTKVDKKIE
A comparison of the crystallographic structures of two catalytic antibodies with esterase activity. Buchbinder, J.L., Stephenson, R.C., Scanlan, T.S. et al. J Mol Biol (1998) 282:1033-1041. DOI 10.1006/jmbi.1998.2025 · PubMed
Other PDB entries of the same protein (UniProt P01837 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 1A0Q directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.