FAB fragment (antibody 8F5) complexed with peptide from human rhinovirus (serotype 2) viral capsid protein VP2 (residues 156-170). Determined by X-ray diffraction at 2.1 Å resolution. Released 29 Apr 1998.
Explore 1A3R in 3D Show helices and sheets RCSB PDB PDBe
1A3R contains 21 α-helices and 45 β-strands across 3 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 | 5-6 | 2 | 7 |
| α-helix | 7-9 | 3 | |
| β-strand | 10-12 | 3 | 8 |
| β-strand | 18-23 | 6 | 7 |
| α-helix | 29-31 | 3 | |
| β-strand | 33-39 | 7 | 8 |
| β-strand | 45-51 | 7 | 8 |
| β-strand | 57-59 | 3 | 8 |
| α-helix | 61-63 | 3 | |
| β-strand | 67-72 | 6 | 7 |
| α-helix | 73-75 | 3 | |
| β-strand | 77-82 | 6 | 7 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-96 | 9 | 8 |
| β-strand | 100A-103 | 4 | 8 |
| β-strand | 107-111 | 5 | 8 |
| α-helix | 114-116 | 3 | |
| β-strand | 117 | 1 | 9 |
| β-strand | 120-124 | 5 | 10 |
| α-helix | 125-127 | 3 | |
| 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 | 171-173 | 3 | 10 |
| α-helix | 174-176 | 3 | |
| β-strand | 177-178 | 2 | 10 |
| β-strand | 185-194 | 10 | 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 | 10-14 | 5 | 2 |
| β-strand | 18-25 | 8 | 1 |
| β-strand | 27C-27D | 2 | 3 |
| β-strand | 30-31 | 2 | 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 | 70-76 | 7 | 1 |
| α-helix | 80-82 | 3 | |
| β-strand | 84-90 | 7 | 2 |
| α-helix | 97 | 1 | |
| β-strand | 98 | 1 | 2 |
| α-helix | 99 | 1 | |
| β-strand | 102-107 | 6 | 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 | 144-150 | 7 | 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 |
| α-helix | 204 | 1 | |
| β-strand | 205-210 | 6 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 164-166 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| IGG2A 8F5 FAB (light chain) | L | protein | 220 | Mus musculus | Q52L64 (AlphaFold model) |
| IGG2A 8F5 FAB (heavy chain) | H | protein | 218 | Mus musculus | Q505N9 (AlphaFold model) |
| Human rhinovirus capsid protein VP2 | P | protein | 16 | Human rhinovirus 2 | P04936 (AlphaFold model) |
>1A3R_1 IGG2A 8F5 FAB (LIGHT CHAIN) (chains L) DIVMTQSPSSLTVTTGEKVTMTCKSSQSLLNSRTQKNYLTWYQQKPGQSPKLLIYWASTR ESGVPDRFTGSGSGTDFTLSISGVQAEDLAVYYCQNNYNYPLTFGAGTKLELKRADAAPT VSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYS MSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>1A3R_2 IGG2A 8F5 FAB (HEAVY CHAIN) (chains H) EVQLQQSGAELVRPGASVKLSCTTSGFNIKDIYIHWVKQRPEQGLEWIGRLDPANGYTKY DPKFQGKATITVDTSSNTAYLHLSSLTSEDTAVYYCDGYYSYYDMDYWGPGTSVTVSSAK TTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDLY TLSSSVTVTSSTWPSQSITCNVAHPASSTKVDKKIEPR
>1A3R_3 HUMAN RHINOVIRUS CAPSID PROTEIN VP2 (chains P) VKAETRLNPDLQPTEX
Crystal structure of a human rhinovirus neutralizing antibody complexed with a peptide derived from viral capsid protein VP2. Tormo, J., Blaas, D., Parry, N.R. et al. EMBO J (1994) 13:2247-2256. PubMed
Other PDB entries of the same protein (UniProt Q52L64 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 1A3R 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.