Crystal Structure Analysis of the germline antibody 36-65 Fab in complex with the dodecapeptide SLGDNLTNHNLR. Determined by X-ray diffraction at 3.0 Å resolution. Released 13 Jun 2006.
Explore 2A6K in 3D Show helices and sheets RCSB PDB PDBe
2A6K contains 25 α-helices and 85 β-strands across 4 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 |
|---|---|---|---|
| α-helix | 2-3 | 2 | |
| β-strand | 4-5 | 2 | 1 |
| β-strand | 10-13 | 4 | 2 |
| β-strand | 20-25 | 6 | 1 |
| β-strand | 33-38 | 6 | 2 |
| β-strand | 44-48 | 5 | 2 |
| β-strand | 49 | 1 | 3 |
| β-strand | 54 | 1 | 3 |
| β-strand | 62-67 | 6 | 1 |
| β-strand | 70-75 | 6 | 1 |
| α-helix | 80-82 | 3 | |
| β-strand | 85-90 | 6 | 2 |
| α-helix | 96 | 1 | |
| β-strand | 97-98 | 2 | 2 |
| β-strand | 102-106 | 5 | 2 |
| β-strand | 114-118 | 5 | 4 |
| α-helix | 122-126 | 5 | |
| β-strand | 129-139 | 11 | 4 |
| β-strand | 145-150 | 6 | 5 |
| β-strand | 153 | 1 | 5 |
| β-strand | 159-163 | 5 | 4 |
| α-helix | 165-167 | 3 | |
| β-strand | 173-182 | 10 | 4 |
| α-helix | 183-187 | 5 | |
| β-strand | 191-198 | 8 | 5 |
| β-strand | 201-210 | 10 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-6 | 4 | 6 |
| α-helix | 7-9 | 3 | |
| β-strand | 10-11 | 2 | 7 |
| β-strand | 17-25 | 9 | 6 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 7 |
| β-strand | 45-52 | 8 | 7 |
| β-strand | 57-60 | 4 | 7 |
| β-strand | 65 | 1 | 6 |
| β-strand | 68-73 | 6 | 6 |
| β-strand | 78-84 | 7 | 6 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-100 | 9 | 7 |
| β-strand | 107-111 | 5 | 7 |
| β-strand | 115-118 | 4 | 7 |
| β-strand | 125 | 1 | 8 |
| β-strand | 128-132 | 5 | 9 |
| β-strand | 143-153 | 11 | 9 |
| β-strand | 154 | 1 | 8 |
| β-strand | 159-162 | 4 | 10 |
| α-helix | 163-165 | 3 | |
| β-strand | 171-173 | 3 | 9 |
| α-helix | 174-176 | 3 | |
| β-strand | 177-178 | 2 | 9 |
| β-strand | 183-192 | 10 | 9 |
| β-strand | 202-207 | 6 | 10 |
| α-helix | 208-210 | 3 | |
| β-strand | 212-217 | 6 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-5 | 3 | 16 |
| α-helix | 6-9 | 4 | |
| β-strand | 10-11 | 2 | 17 |
| β-strand | 18-20 | 3 | 16 |
| β-strand | 23-25 | 3 | 16 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 17 |
| β-strand | 45-51 | 7 | 17 |
| β-strand | 58-60 | 3 | 17 |
| β-strand | 65 | 1 | 16 |
| β-strand | 68-73 | 6 | 16 |
| β-strand | 78-83 | 6 | 16 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-103 | 12 | 17 |
| β-strand | 105-111 | 7 | 17 |
| β-strand | 115-118 | 4 | 17 |
| β-strand | 125 | 1 | 18 |
| β-strand | 128-132 | 5 | 19 |
| β-strand | 143-153 | 11 | 19 |
| β-strand | 154 | 1 | 18 |
| β-strand | 159-162 | 4 | 20 |
| α-helix | 163-165 | 3 | |
| β-strand | 172-173 | 2 | 19 |
| α-helix | 174-176 | 3 | |
| β-strand | 177-178 | 2 | 19 |
| β-strand | 183-192 | 10 | 19 |
| β-strand | 202-207 | 6 | 20 |
| α-helix | 208-210 | 3 | |
| β-strand | 212-217 | 6 | 20 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5 | 1 | 11 |
| β-strand | 10-13 | 4 | 12 |
| β-strand | 20-24 | 5 | 11 |
| β-strand | 33-38 | 6 | 12 |
| β-strand | 44-48 | 5 | 12 |
| β-strand | 49 | 1 | 13 |
| β-strand | 54 | 1 | 13 |
| β-strand | 62-67 | 6 | 11 |
| β-strand | 70-75 | 6 | 11 |
| α-helix | 80-82 | 3 | |
| β-strand | 85-90 | 6 | 12 |
| α-helix | 96 | 1 | |
| β-strand | 97-98 | 2 | 12 |
| β-strand | 102-106 | 5 | 12 |
| β-strand | 114-118 | 5 | 14 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-125 | 4 | |
| β-strand | 129-139 | 11 | 14 |
| β-strand | 145-150 | 6 | 15 |
| β-strand | 154-155 | 2 | 15 |
| β-strand | 159-163 | 5 | 14 |
| α-helix | 164-167 | 4 | |
| β-strand | 173-182 | 10 | 14 |
| α-helix | 183-186 | 4 | |
| β-strand | 191-197 | 7 | 15 |
| α-helix | 204 | 1 | |
| β-strand | 205-210 | 6 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Germline antibody 36-65 Fab light chain | A, L | protein | 214 | Mus musculus | P01837 (AlphaFold model) |
| Germline antibody 36-65 Fab heavy chain | B, H | protein | 222 | Mus musculus | Q6PF95 (AlphaFold model) |
| Dodecapeptide: slgdnltnhnlr | P | protein | 12 |
>2A6K_1 Germline antibody 36-65 Fab light chain (chains A, L) DIQMTQTTSSLSASLGDRVTISCRASQDISNYLNWYQQKPDGTVKLLIYYTSRLHSGVPS RFSGSGSGTDYSLTISNLEQEDIATYFCQQGNTLPRTFGGGTKLEIKRADAAPTVSIFPP SSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLT LTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>2A6K_2 Germline antibody 36-65 Fab heavy chain (chains B, H) EVQLQQSGAELVRAGSSVKMSCKASGYTFTSYGINWVKQRPGQGLEWIGYINPGNGYTKY NEKFKGKTTLTVDKSSSTAYMQLRSLTSEDSAVYFCARSVYYGGSYYFDYWGQGTTLTVS SAKTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQS DLYTLSSSVTVPSSPRPSETVTCNVAHPASSTKVDKKIVPRD
>2A6K_3 DODECAPEPTIDE: SLGDNLTNHNLR (chains P) SLGDNLTNHNLR
Differential epitope positioning within the germline antibody paratope enhances promiscuity in the primary immune response. Sethi, D.K., Agarwal, A., Manivel, V. et al. Immunity (2006) 24:429-438. DOI 10.1016/j.immuni.2006.02.010 · PubMed
Other PDB entries of the same protein (UniProt P01837 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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