OPG2 FAB fragment. Determined by X-ray diffraction at 2.0 Å resolution. Released 31 Jul 1995.
Explore 1OPG in 3D Show helices and sheets RCSB PDB PDBe
1OPG contains 11 α-helices and 43 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 | 34-39 | 6 | 9 |
| β-strand | 45-51 | 7 | 9 |
| β-strand | 59 | 1 | 9 |
| β-strand | 68-73 | 6 | 7 |
| β-strand | 78-83 | 6 | 7 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-98 | 7 | 9 |
| β-strand | 114-115 | 2 | 9 |
| β-strand | 119-121 | 3 | 9 |
| β-strand | 122-123 | 2 | 8 |
| β-strand | 129 | 1 | 10 |
| β-strand | 132-136 | 5 | 11 |
| β-strand | 147-157 | 11 | 11 |
| β-strand | 158 | 1 | 10 |
| β-strand | 163-166 | 4 | 12 |
| α-helix | 167-169 | 3 | |
| β-strand | 175-183 | 9 | 11 |
| β-strand | 186-196 | 11 | 11 |
| β-strand | 206-211 | 6 | 12 |
| α-helix | 212-214 | 3 | |
| β-strand | 216-221 | 6 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 1 |
| β-strand | 12-13 | 2 | 2 |
| β-strand | 19-25 | 7 | 1 |
| β-strand | 33-38 | 6 | 3 |
| β-strand | 45-49 | 5 | 3 |
| α-helix | 50-52 | 3 | |
| β-strand | 53-54 | 2 | 3 |
| β-strand | 62-67 | 6 | 1 |
| β-strand | 70-75 | 6 | 1 |
| α-helix | 80-82 | 3 | |
| β-strand | 85-90 | 6 | 3 |
| α-helix | 96 | 1 | |
| β-strand | 97-98 | 2 | 3 |
| β-strand | 102-103 | 2 | 3 |
| β-strand | 105-106 | 2 | 2 |
| β-strand | 111 | 1 | 4 |
| β-strand | 114-118 | 5 | 5 |
| α-helix | 119-121 | 3 | |
| α-helix | 125-127 | 3 | |
| 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 |
| β-strand | 173-182 | 10 | 5 |
| α-helix | 183-186 | 4 | |
| β-strand | 191-198 | 8 | 6 |
| α-helix | 204 | 1 | |
| β-strand | 205-210 | 6 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| OPG2 FAB (light chain) | L | protein | 214 | Homo sapiens | |
| OPG2 FAB (heavy chain) | H | protein | 227 | Homo sapiens | P01868 (AlphaFold model) |
>1OPG_1 OPG2 FAB (LIGHT CHAIN) (chains L) DELLTQSPATLSVTPGDSVSLSCRASQSISNNLHWYQQKSHESPRLLIKYASQSISGIPS RFSGSGSGTDFTLSINSVETEDFGMYFCQQSNSWPLTFGGGSKLEIKRADAAPTVSIFPP SSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLT LTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>1OPG_2 OPG2 FAB (HEAVY CHAIN) (chains H) EVQLVQSGGGLVNPGRSLKLSCAASGFTFSSYGMSWVRQTPEKRLEWVAAISGGGTYIHY PDSVKGRFTISRDNAKNNLYLQMSSLRSEDTALYYCTRHPFYRYDGGNYYAMDHWGQGTS VTVSAAKTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPA VLQSDLYTLSSSVTVPSSPRPSETVTCNVAHPASSTKVDKKIVPRDC
Crystal structure of the OPG2 Fab. An antireceptor antibody that mimics an RGD cell adhesion site. Kodandapani, R., Veerapandian, B., Kunicki, T.J. et al. J Biol Chem (1995) 270:2268-2273. DOI 10.1074/jbc.270.5.2268 · PubMed
Other PDB entries of the same protein (UniProt P01868 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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