5FBZ: Enzyme subtilase SubHal from Bacillus halmapalus
Structure of subtilase SubHal from Bacillus halmapalus - complex with chymotrypsin inhibitor CI2A. Determined by X-ray diffraction at 1.9 Å resolution. Released 18 May 2016.
- Method
- X-ray diffraction
- Resolution
- 1.9 Å
- Organisms
- Bacillus halmapalus, Hordeum vulgare
- Chains
- 5
- Atoms
- 8,682
- Mol. weight
- 107.73 kDa
- Ligands
- CA
- Released
- 18 May 2016
Explore 5FBZ in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
5FBZ contains 40 α-helices and 74 β-strands across 5 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.
Chain A: 18 helices, 28 β-strands
| 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 |
| α-helix | 110-119 | 10 | |
| β-strand | 124-127 | 4 | 1 |
| β-strand | 129-130 | 2 | 2 |
| 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 | |
| β-strand | 201 | 1 | 1 |
| α-helix | 202 | 1 | |
| β-strand | 219-222 | 4 | 1 |
| β-strand | 226-229 | 4 | 4 |
| α-helix | 230-231 | 2 | |
| α-helix | 236-238 | 3 | |
| β-strand | 241-244 | 4 | 4 |
| β-strand | 247-250 | 4 | 4 |
| β-strand | 252 | 1 | 5 |
| α-helix | 253-274 | 22 | |
| α-helix | 281-291 | 11 | |
| α-helix | 292 | 1 | |
| β-strand | 293 | 1 | 1 |
| α-helix | 294 | 1 | |
| β-strand | 308 | 1 | 1 |
| α-helix | 311-315 | 5 | |
| β-strand | 318-321 | 4 | 6 |
| β-strand | 326 | 1 | 7 |
| β-strand | 331-338 | 8 | 8 |
| β-strand | 344-349 | 6 | 6 |
| α-helix | 352-356 | 5 | |
| β-strand | 366-372 | 7 | 8 |
| β-strand | 378-380 | 3 | 8 |
| β-strand | 385 | 1 | 9 |
| β-strand | 398-403 | 6 | 6 |
| α-helix | 406-407 | 2 | |
| β-strand | 409-419 | 11 | 8 |
| β-strand | 425 | 1 | 7 |
| β-strand | 428-432 | 5 | 6 |
Chain B: 2 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 23 | 1 | 10 |
| α-helix | 25-27 | 3 | |
| β-strand | 31 | 1 | 11 |
| α-helix | 32-42 | 11 | |
| β-strand | 47-52 | 6 | 10 |
| β-strand | 57-58 | 2 | 2 |
| β-strand | 60 | 1 | 5 |
| β-strand | 65-70 | 6 | 10 |
| β-strand | 75 | 1 | 11 |
| β-strand | 76 | 1 | 10 |
| β-strand | 81-82 | 2 | 10 |
Chain C: 16 helices, 27 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-7 | 6 | |
| α-helix | 10-17 | 8 | |
| β-strand | 25-30 | 6 | 12 |
| β-strand | 50-55 | 6 | 12 |
| α-helix | 68-77 | 10 | |
| β-strand | 90-95 | 6 | 12 |
| α-helix | 110-119 | 10 | |
| β-strand | 124-127 | 4 | 12 |
| β-strand | 129-130 | 2 | 13 |
| β-strand | 131 | 1 | 14 |
| α-helix | 139-150 | 12 | |
| β-strand | 154-158 | 5 | 12 |
| α-helix | 169-170 | 2 | |
| β-strand | 171 | 1 | 14 |
| β-strand | 179-184 | 6 | 12 |
| α-helix | 189-191 | 3 | |
| β-strand | 192 | 1 | 9 |
| α-helix | 193-195 | 3 | |
| α-helix | 200 | 1 | |
| β-strand | 201 | 1 | 12 |
| α-helix | 202 | 1 | |
| β-strand | 219-222 | 4 | 12 |
| β-strand | 226-229 | 4 | 15 |
| α-helix | 236-238 | 3 | |
| β-strand | 241-242 | 2 | 15 |
| β-strand | 247-250 | 4 | 15 |
| α-helix | 253-274 | 22 | |
| α-helix | 281-291 | 11 | |
| β-strand | 293 | 1 | 12 |
| β-strand | 308 | 1 | 12 |
| α-helix | 311-315 | 5 | |
| β-strand | 318-321 | 4 | 16 |
| β-strand | 326 | 1 | 17 |
| β-strand | 331-338 | 8 | 18 |
| β-strand | 344-349 | 6 | 16 |
| α-helix | 352-354 | 3 | |
| β-strand | 366-372 | 7 | 18 |
| β-strand | 378-380 | 3 | 18 |
| β-strand | 398-403 | 6 | 16 |
| α-helix | 406-407 | 2 | |
| β-strand | 409-419 | 11 | 18 |
| β-strand | 425 | 1 | 17 |
| β-strand | 428-432 | 5 | 16 |
Chain D: 2 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 23 | 1 | 19 |
| α-helix | 25-27 | 3 | |
| β-strand | 31 | 1 | 20 |
| α-helix | 32-42 | 11 | |
| β-strand | 47-52 | 6 | 21 |
| β-strand | 57-58 | 2 | 13 |
| β-strand | 65-70 | 6 | 21 |
| β-strand | 75 | 1 | 20 |
| β-strand | 76 | 1 | 21 |
| β-strand | 81 | 1 | 19 |
| β-strand | 82 | 1 | 21 |
Chain E: 2 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 281 | 1 | |
| β-strand | 282 | 1 | 8 |
| α-helix | 283 | 1 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Enzyme subtilase SubHal from Bacillus halmapalus | A, C | protein | 433 | Bacillus halmapalus | A0A182DWC7 (AlphaFold model) |
| Subtilisin-chymotrypsin inhibitor-2A | B, D | protein | 72 | Hordeum vulgare | P01053 (AlphaFold model) |
| Autoproteolytic fragment of enzyme subtilase SubHal | E | protein | 5 | Bacillus halmapalus | |
Sequence of entity 1 (A, C), FASTA
>5FBZ_1 Enzyme subtilase SubHal from Bacillus halmapalus (chains A, C)
NDVARGIVKADVAQNNFGLYGQGQIVAVADTGLDTGRNDSSMHEAFRGKITALYALGRTN
NANDPNGHGTHVAGSVLGNATNKGMAPQANLVFQSIMDSGGGLGGLPANLQTLFSQAYSA
GARIHTNSWGAPVNGAYTTDSRNVDDYVRKNDMTILFAAGNEGPGSGTISAPGTAKNAIT
VGATENLRPSFGSYADNINHVAQFSSRGPTRDGRIKPDVMAPGTYILSARSSLAPDSSFW
ANHDSKYAYMGGTSMATPIVAGNVAQLREHFVKNRGVTPKPSLLKAALIAGAADVGLGFP
NGNQGWGRVTLDKSLNVAFVNETSPLSTSQKATYSFTAQAGKPLKISLVWSDAPGSTTAS
LTLVNDLDLVITAPNGTKYVGNDFTAPYDNNWDGRNNVENVFINAPQSGTYTVEVQAYNV
PVGPQTFSLAIVH
Sequence of entity 2 (B, D), FASTA
>5FBZ_2 Subtilisin-chymotrypsin inhibitor-2A (chains B, D)
TGAGDRHNLKTEWPELVGKSVEEAKKVILQDKPEAQIIVLPVGTIVTMEYRIDRVRLFVD
KLDNIAEVPRVG
Sequence of entity 3 (E), FASTA
>5FBZ_3 Autoproteolytic fragment of enzyme subtilase SubHal (chains E)
KPSLL
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| CA | Calcium ion | Ca | 6 |
Primary citation
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:
- 5FAX 2.0 Å, Structure of subtilase SubHal from Bacillus halmapalus
Browse structure collections
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