NMR structure of SARS-CoV non-structural protein NSP3A (SARS1) from SARS coronavirus. Determined by X-ray diffraction at 1.4 Å resolution. Released 14 Feb 2006.
Explore 2ACF in 3D Show helices and sheets RCSB PDB PDBe
2ACF contains 43 α-helices and 28 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 |
|---|---|---|---|
| β-strand | 192-193 | 2 | 1 |
| β-strand | 198-202 | 5 | 1 |
| α-helix | 205-212 | 8 | |
| β-strand | 216-220 | 5 | 1 |
| α-helix | 230-238 | 9 | |
| α-helix | 242-254 | 13 | |
| β-strand | 262-266 | 5 | 1 |
| β-strand | 273-277 | 5 | 1 |
| α-helix | 282-284 | 3 | |
| α-helix | 288-290 | 3 | |
| α-helix | 291-296 | 6 | |
| α-helix | 297-300 | 4 | |
| β-strand | 303-306 | 4 | 1 |
| α-helix | 307-308 | 2 | |
| α-helix | 312-314 | 3 | |
| α-helix | 318-328 | 11 | |
| β-strand | 332-337 | 6 | 1 |
| α-helix | 340-350 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 191 | 1 | |
| β-strand | 192-193 | 2 | 2 |
| β-strand | 198-202 | 5 | 2 |
| α-helix | 205-212 | 8 | |
| β-strand | 216-220 | 5 | 2 |
| α-helix | 230-238 | 9 | |
| α-helix | 242-254 | 13 | |
| β-strand | 262-266 | 5 | 2 |
| β-strand | 273-277 | 5 | 2 |
| α-helix | 282-284 | 3 | |
| α-helix | 290-296 | 7 | |
| α-helix | 297-300 | 4 | |
| β-strand | 303-306 | 4 | 2 |
| α-helix | 307-308 | 2 | |
| α-helix | 312-314 | 3 | |
| α-helix | 318-328 | 11 | |
| β-strand | 332-337 | 6 | 2 |
| α-helix | 340-353 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 192-193 | 2 | 3 |
| β-strand | 198-202 | 5 | 3 |
| α-helix | 205-212 | 8 | |
| β-strand | 216-220 | 5 | 3 |
| α-helix | 230-238 | 9 | |
| α-helix | 242-254 | 13 | |
| β-strand | 262-266 | 5 | 3 |
| β-strand | 273-277 | 5 | 3 |
| α-helix | 288-290 | 3 | |
| α-helix | 291-296 | 6 | |
| α-helix | 297-300 | 4 | |
| β-strand | 303-306 | 4 | 3 |
| α-helix | 307-308 | 2 | |
| α-helix | 312-314 | 3 | |
| α-helix | 318-328 | 11 | |
| β-strand | 332-337 | 6 | 3 |
| α-helix | 340-354 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Replicase polyprotein 1ab | A, B, C, D | protein | 182 | SARS coronavirus Tor2 | P0C6X7 (AlphaFold model) |
>2ACF_1 Replicase polyprotein 1ab (chains A, B, C, D) HHHHHHMPVNQFTGYLKLTDNVAIKCVDIVKEAQSANPMVIVNAANIHLKHGGGVAGALN KATNGAMQKESDDYIKLNGPLTVGGSCLLSGHNLAKKCLHVVGPNLNAGEDIQLLKAAYE NFNSQDILLAPLLSAGIFGAKPLQSLQVCVQTVRTQVYIAVNDKALYEQVVMDYLDNLKP RV
Structural basis of severe acute respiratory syndrome coronavirus ADP-ribose-1''-phosphate dephosphorylation by a conserved domain of nsP3. Saikatendu, K.S., Joseph, J.S., Subramanian, V. et al. Structure (2005) 13:1665-1675. DOI 10.1016/j.str.2005.07.022 · PubMed
Other PDB entries of the same protein (UniProt P0C6X7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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