Crystal structure of MJF14-6-4-2 Fab fragment in complex with epitope peptide. Determined by X-ray diffraction at 1.71 Å resolution. Released 27 Mar 2024.
Explore 8OG0 in 3D Show helices and sheets RCSB PDB PDBe
8OG0 contains 19 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 | 6 |
| β-strand | 11-12 | 2 | 7 |
| β-strand | 18-25 | 8 | 6 |
| β-strand | 33-40 | 8 | 8 |
| β-strand | 46-53 | 8 | 8 |
| β-strand | 60-62 | 3 | 8 |
| α-helix | 64-66 | 3 | |
| β-strand | 70-76 | 7 | 6 |
| β-strand | 79-84 | 6 | 6 |
| α-helix | 89-91 | 3 | |
| β-strand | 93-101 | 9 | 8 |
| α-helix | 102 | 1 | |
| α-helix | 106-109 | 4 | |
| β-strand | 111-112 | 2 | 8 |
| β-strand | 116-118 | 3 | 8 |
| β-strand | 119-120 | 2 | 7 |
| β-strand | 126 | 1 | 9 |
| α-helix | 127-128 | 2 | |
| β-strand | 129-133 | 5 | 10 |
| β-strand | 146-154 | 9 | 10 |
| β-strand | 155 | 1 | 9 |
| β-strand | 160-163 | 4 | 11 |
| α-helix | 164-166 | 3 | |
| β-strand | 168 | 1 | 11 |
| β-strand | 172-174 | 3 | 10 |
| α-helix | 175-177 | 3 | |
| β-strand | 178-179 | 2 | 10 |
| β-strand | 185-192 | 8 | 10 |
| β-strand | 202-207 | 6 | 11 |
| α-helix | 208-210 | 3 | |
| β-strand | 212-217 | 6 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-5 | 3 | 1 |
| β-strand | 9-13 | 5 | 2 |
| β-strand | 18-24 | 7 | 1 |
| α-helix | 27-28 | 2 | |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 2 |
| β-strand | 46-50 | 5 | 2 |
| β-strand | 54-55 | 2 | 2 |
| α-helix | 56 | 1 | |
| β-strand | 63-68 | 6 | 1 |
| β-strand | 71-76 | 6 | 1 |
| α-helix | 81-83 | 3 | |
| β-strand | 85-92 | 8 | 2 |
| β-strand | 101-103 | 3 | 2 |
| β-strand | 107-112 | 6 | 2 |
| β-strand | 116 | 1 | 3 |
| α-helix | 117-118 | 2 | |
| β-strand | 119-123 | 5 | 4 |
| α-helix | 124-126 | 3 | |
| α-helix | 127-130 | 4 | |
| β-strand | 134-144 | 11 | 4 |
| β-strand | 145 | 1 | 3 |
| β-strand | 149-154 | 6 | 5 |
| β-strand | 157-158 | 2 | 5 |
| α-helix | 159 | 1 | |
| β-strand | 163-167 | 5 | 4 |
| α-helix | 168-171 | 4 | |
| β-strand | 177-186 | 10 | 4 |
| α-helix | 187-190 | 4 | |
| β-strand | 195-202 | 8 | 5 |
| β-strand | 205-212 | 8 | 5 |
| α-helix | 213-215 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Fab fragment light chain | L | protein | 216 | Oryctolagus cuniculus | |
| Fab fragment heavy chain | H | protein | 222 | Oryctolagus cuniculus | |
| Alpha-synuclein | P | protein | 5 | Homo sapiens | P37840 (AlphaFold model) |
>8OG0_1 Fab fragment light chain (chains L) QVLTQTASSVSAAVGGTVTISCQSSQSVYKNNYLAWYQQKPGQPPNLLIYNASTLASGVS SRFRGSGSGTQFTLTISGVQCDDAATYYCQGGFPCRTADCNVFGGGTEVVVKGDPVAPTV LIFPPAADQVATGTVTIVCVANKYFPDVTVTWEVDGTTQTTGIENSKTPQNSADCTYNLS STLTLTSTQYNSHKEYTCKVTQGTTSVVQSFNRGDC
>8OG0_2 Fab fragment heavy chain (chains H) QEQLVESGGDLVKPGASLTLTCTASGFSFSSNYWMCWFRQAPGKGPEWIACIYAGNSGST YYATWAKGRFTISKTSSTTVTLQMTSLTAADTATYFCWRRGAYGYYGDLNLWGPGTLVTV SSGQPKAPSVFPLAPCCGDTPSSTVTLGCLVKGYLPEPVTVTWNSGTLTNGVRTFPSVRQ SSGLYSLSSVVSVTSSSQPEVTCNVAHPATNTKVDKTVAPST
>8OG0_3 Alpha-synuclein (chains P) YEPEA
Structural basis of epitope recognition by anti-alpha-synuclein antibodies MJFR14-6-4-2. Lieknina, I., Reimer, L., Pantelejevs, T. et al. NPJ Parkinsons Dis (2024) 10:206-206. DOI 10.1038/s41531-024-00822-y · PubMed
Other PDB entries of the same protein (UniProt P37840 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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