Structure of subtilase SubHal from Bacillus halmapalus. Determined by X-ray diffraction at 2.0 Å resolution. Released 18 May 2016.
Explore 5FAX in 3D Show helices and sheets RCSB PDB PDBe
5FAX contains 31 α-helices and 52 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 |
|---|---|---|---|
| α-helix | 2-7 | 6 | |
| α-helix | 10-17 | 8 | |
| β-strand | 25-30 | 6 | 1 |
| β-strand | 50-55 | 6 | 1 |
| α-helix | 68-77 | 10 | |
| β-strand | 90-95 | 6 | 1 |
| β-strand | 107 | 1 | 2 |
| α-helix | 111-119 | 9 | |
| β-strand | 124-127 | 4 | 1 |
| β-strand | 131 | 1 | 3 |
| α-helix | 139-150 | 12 | |
| β-strand | 154-158 | 5 | 1 |
| α-helix | 169-170 | 2 | |
| β-strand | 171 | 1 | 3 |
| β-strand | 179-184 | 6 | 1 |
| α-helix | 189-191 | 3 | |
| α-helix | 193-195 | 3 | |
| α-helix | 200 | 1 | |
| β-strand | 201 | 1 | 1 |
| α-helix | 202 | 1 | |
| β-strand | 219-222 | 4 | 1 |
| β-strand | 226-229 | 4 | 4 |
| α-helix | 236-238 | 3 | |
| β-strand | 241-242 | 2 | 4 |
| β-strand | 247-250 | 4 | 4 |
| α-helix | 253-274 | 22 | |
| α-helix | 281-291 | 11 | |
| β-strand | 293 | 1 | 1 |
| β-strand | 308 | 1 | 1 |
| α-helix | 311-315 | 5 | |
| β-strand | 318-321 | 4 | 5 |
| β-strand | 326 | 1 | 6 |
| β-strand | 331-338 | 8 | 7 |
| β-strand | 344-349 | 6 | 5 |
| α-helix | 352-354 | 3 | |
| β-strand | 366-372 | 7 | 7 |
| β-strand | 378-380 | 3 | 7 |
| β-strand | 398-403 | 6 | 5 |
| α-helix | 406-407 | 2 | |
| β-strand | 409-419 | 11 | 7 |
| β-strand | 425 | 1 | 6 |
| β-strand | 428-432 | 5 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-7 | 6 | |
| α-helix | 10-15 | 6 | |
| β-strand | 25-30 | 6 | 8 |
| β-strand | 50-55 | 6 | 8 |
| α-helix | 68-77 | 10 | |
| β-strand | 90-95 | 6 | 8 |
| β-strand | 107 | 1 | 2 |
| α-helix | 110-119 | 10 | |
| β-strand | 124-127 | 4 | 8 |
| β-strand | 131 | 1 | 9 |
| α-helix | 139-150 | 12 | |
| β-strand | 154-158 | 5 | 8 |
| α-helix | 169-170 | 2 | |
| β-strand | 171 | 1 | 9 |
| β-strand | 179-184 | 6 | 8 |
| α-helix | 185-186 | 2 | |
| α-helix | 189-191 | 3 | |
| β-strand | 201 | 1 | 8 |
| β-strand | 219-222 | 4 | 8 |
| β-strand | 226-229 | 4 | 10 |
| α-helix | 236-238 | 3 | |
| β-strand | 241-242 | 2 | 10 |
| β-strand | 247-250 | 4 | 10 |
| α-helix | 253-270 | 18 | |
| α-helix | 271-275 | 5 | |
| α-helix | 281-291 | 11 | |
| β-strand | 293 | 1 | 8 |
| β-strand | 308 | 1 | 8 |
| α-helix | 311-315 | 5 | |
| β-strand | 318-321 | 4 | 11 |
| β-strand | 326 | 1 | 12 |
| β-strand | 331-338 | 8 | 13 |
| β-strand | 344-349 | 6 | 11 |
| α-helix | 352-354 | 3 | |
| β-strand | 366-372 | 7 | 13 |
| β-strand | 378-380 | 3 | 13 |
| β-strand | 398-403 | 6 | 11 |
| α-helix | 406-407 | 2 | |
| β-strand | 409-419 | 11 | 13 |
| β-strand | 425 | 1 | 12 |
| β-strand | 428-432 | 5 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Subtilase SubHal from Bacillus halmapalus | A, B | protein | 433 | Bacillus halmapalus | A0A182DWC7 (AlphaFold model) |
>5FAX_1 Subtilase SubHal from Bacillus halmapalus (chains A, B) NDVARGIVKADVAQNNFGLYGQGQIVAVADTGLDTGRNDSSMHEAFRGKITALYALGRTN NANDPNGHGTHVAGSVLGNATNKGMAPQANLVFQSIMDSGGGLGGLPANLQTLFSQAYSA GARIHTNSWGAPVNGAYTTDSRNVDDYVRKNDMTILFAAGNEGPGSGTISAPGTAKNAIT VGATENLRPSFGSYADNINHVAQFSSRGPTRDGRIKPDVMAPGTYILSARSSLAPDSSFW ANHDSKYAYMGGTSMATPIVAGNVAQLREHFVKNRGVTPKPSLLKAALIAGAADVGLGFP NGNQGWGRVTLDKSLNVAFVNETSPLSTSQKATYSFTAQAGKPLKISLVWSDAPGSTTAS LTLVNDLDLVITAPNGTKYVGNDFTAPYDNNWDGRNNVENVFINAPQSGTYTVEVQAYNV PVGPQTFSLAIVH
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 6 |
Stabilization of Enzymes by Metal Binding: Structures of Two Alkalophilic Bacillus Subtilases and Analysis of the Second Metal-Binding Site of the Subtilase Family. Dohnalek, J., McAuley, K.E., Brzozowski, A.M. et al. Book (2016):203-266. DOI 10.4032/9789814669337
Other PDB entries of the same protein (UniProt A0A182DWC7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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