Crystal structure of human 5' exonuclease Apollo. Determined by X-ray diffraction at 2.16 Å resolution. Released 18 Feb 2015.
Explore 5AHO in 3D Show helices and sheets RCSB PDB PDBe
5AHO contains 14 α-helices and 19 β-strands across 1 chain. 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 | 4-6 | 3 | 1 |
| β-strand | 11-13 | 3 | 1 |
| α-helix | 18-21 | 4 | |
| β-strand | 26-28 | 3 | 1 |
| α-helix | 34-36 | 3 | |
| β-strand | 48-50 | 3 | 1 |
| α-helix | 52-61 | 10 | |
| β-strand | 69-71 | 3 | 1 |
| β-strand | 77-81 | 5 | 2 |
| β-strand | 89-96 | 8 | 2 |
| β-strand | 104-110 | 7 | 2 |
| β-strand | 113-117 | 5 | 2 |
| α-helix | 125-129 | 5 | |
| α-helix | 131-133 | 3 | |
| β-strand | 141-144 | 4 | 2 |
| β-strand | 148 | 1 | 3 |
| α-helix | 158-170 | 13 | |
| β-strand | 176-181 | 6 | 4 |
| α-helix | 187-196 | 10 | |
| α-helix | 200 | 1 | |
| β-strand | 201-202 | 2 | 4 |
| α-helix | 205-214 | 10 | |
| β-strand | 220-221 | 2 | 4 |
| α-helix | 224-226 | 3 | |
| β-strand | 229-233 | 5 | 4 |
| α-helix | 234-236 | 3 | |
| α-helix | 239-245 | 7 | |
| β-strand | 251-256 | 6 | 4 |
| β-strand | 268-271 | 4 | 4 |
| β-strand | 278 | 1 | 3 |
| α-helix | 279-289 | 11 | |
| β-strand | 294-296 | 3 | 2 |
| α-helix | 307-309 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 5' exonuclease apollo | A | protein | 336 | HOMO SAPIENS | Q9H816 (AlphaFold model) |
>5AHO_1 5' EXONUCLEASE APOLLO (chains A) SMNGVLIPHTPIAVDFWSLRRAGTARLFFLSHMHSDHTVGLSSTWARPLYCSPITAHLLH RHLQVSKQWIQALEVGESHVLPLDEIGQETMTVTLLDANHCPGSVMFLFEGYFGTILYTG DFRYTPSMLKEPALTLGKQIHTLYLDNTNCNPALVLPSRQEAAHQIVQLIRKHPQHNIKI GLYSLGKESLLEQLALEFQTWVVLSPRRLELVQLLGLADVFTVEEKAGRIHAVDHMEICH SNMLRWNQTHPTIAILPTSRKIHSSHPDIHVIPYSDHSSYSELRAFVAALKPCQVVPIVS RRPCGGFQDSLSPRISVPLIPDSVQQYMSSFSRKPS
Water and common crystallization additives (EDO) are not listed.
The Structures of the Snm1A and Snm1B/Apollo Nuclease Domains Reveal a Potential Basis for Their Distinct DNA Processing Activities. Allerston, C.K., Lee, S.Y., Newman, J.A. et al. Nucleic Acids Res (2015) 43:11047. DOI 10.1093/NAR/GKV1256 · PubMed
Other PDB entries of the same protein (UniProt Q9H816 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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