Research workbench
The crystal structure of the bacillus lentus alkaline protease, subtilisin bl, at 1.4 ångströms resolution
Analyse The crystal structure of the bacillus lentus alkaline protease, subtilisin bl… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ST3
- Type
- protein
- Length
- 269 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Subtilisin bl
- EC
- 3.4.21.62
- UniProt
- P29599
- Ligands
- CA
- Pockets
- 1 · best druggability 0.36
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Subtilisin bl (EC 3.4.21.62) | protein | 269 | 30% helix, 20% strand | P29599 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 85 | 0.36 | 0.76 | 23 | empty |
Compared structures
- 1ST3 · The crystal structure of the bacillus lentus alkaline protease, subtilisin bl, at 1.4… · the same entry in another collection · chain A against A, TM-score 1.00
- P29599 · AlphaFold monomer V2.0 prediction for subtilisin bl (P29599) · a predicted model of the same protein · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P29599
- Elsewhere: RCSB PDB 1ST3 · PDBe 1ST3 · UniProt P29599
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