Rabbit muscle Aldolase (D2 symmetry) determined using the TFS Vitrobot Mark IV in the presence of 1x SurfACT. Determined by electron microscopy at 1.98 Å resolution. Released 8 Apr 2026.
Explore 11NX in 3D Show helices and sheets RCSB PDB PDBe
11NX contains 71 α-helices and 56 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 | 9-22 | 14 | |
| β-strand | 28-32 | 5 | 1 |
| α-helix | 36-44 | 9 | |
| α-helix | 52-63 | 12 | |
| α-helix | 67-69 | 3 | |
| β-strand | 73-78 | 6 | 1 |
| α-helix | 80-83 | 4 | |
| β-strand | 86 | 1 | 2 |
| β-strand | 92 | 1 | 2 |
| α-helix | 93-99 | 7 | |
| α-helix | 102 | 1 | |
| β-strand | 103-107 | 5 | 1 |
| β-strand | 112-114 | 3 | 3 |
| α-helix | 115 | 1 | |
| β-strand | 122-124 | 3 | 3 |
| α-helix | 130-139 | 10 | |
| β-strand | 144-151 | 8 | 1 |
| α-helix | 160-179 | 20 | |
| β-strand | 183-190 | 8 | 1 |
| α-helix | 191 | 1 | |
| α-helix | 198-218 | 21 | |
| α-helix | 223-225 | 3 | |
| β-strand | 227-228 | 2 | 1 |
| β-strand | 231 | 1 | 4 |
| α-helix | 245-259 | 15 | |
| β-strand | 266-269 | 4 | 1 |
| β-strand | 270 | 1 | 4 |
| α-helix | 276-287 | 12 | |
| β-strand | 296-301 | 6 | 1 |
| α-helix | 303-313 | 11 | |
| α-helix | 317-319 | 3 | |
| α-helix | 320-337 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 9-22 | 14 | |
| β-strand | 28-32 | 5 | 5 |
| α-helix | 36-44 | 9 | |
| α-helix | 52-63 | 12 | |
| α-helix | 67-69 | 3 | |
| β-strand | 73-78 | 6 | 5 |
| α-helix | 80-83 | 4 | |
| β-strand | 86 | 1 | 6 |
| β-strand | 92 | 1 | 6 |
| α-helix | 93-99 | 7 | |
| β-strand | 103-107 | 5 | 5 |
| β-strand | 112-114 | 3 | 7 |
| α-helix | 115 | 1 | |
| β-strand | 122-124 | 3 | 7 |
| α-helix | 130-139 | 10 | |
| β-strand | 144-151 | 8 | 5 |
| α-helix | 160-179 | 20 | |
| β-strand | 183-190 | 8 | 5 |
| α-helix | 191 | 1 | |
| α-helix | 198-218 | 21 | |
| α-helix | 223-225 | 3 | |
| β-strand | 227-228 | 2 | 5 |
| β-strand | 231 | 1 | 8 |
| α-helix | 245-259 | 15 | |
| β-strand | 266-269 | 4 | 5 |
| β-strand | 270 | 1 | 8 |
| α-helix | 276-287 | 12 | |
| β-strand | 296-301 | 6 | 5 |
| α-helix | 303-313 | 11 | |
| α-helix | 317-319 | 3 | |
| α-helix | 320-337 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Fructose-bisphosphate aldolase A | A, B, C, D | protein | 343 | Oryctolagus cuniculus | P00883 (AlphaFold model) |
>11NX_1 Fructose-bisphosphate aldolase A (chains A, B, C, D) HSHPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQL LLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGE TTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYASICQQNG IVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQ KYSHEEIAMATVTALRRTVPPAVTGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFSY GRALQASALKAWGGKKENLKAAQEEYVKRALANSLACQGKYTP
A Surfactant Cocktail Overcomes Air-Water Interface Artifacts in Single-Particle CryoEM. Enos, S.E., Cook, B.D., Rahmani, H. et al. bioRxiv (2026). DOI 10.64898/2026.03.17.712260 · PubMed
Other PDB entries of the same protein (UniProt P00883 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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