Research workbench
Subtilisin bpn' from bacillus amyloliquefaciens, mutant
Analyse Subtilisin bpn' from bacillus amyloliquefaciens, mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SUE
- Type
- protein
- Length
- 266 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.8
- Source
- Bacillus amyloliquefaciens
- Molecule
- Subtilisin bpn'
- EC
- 3.4.21.62
- UniProt
- P00782
- Ligands
- DFP, NA
- Pockets
- 1 · best druggability 0.38
Structure
x-ray diffraction · resolution 1.8 · 1 distinct chain · 32% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Subtilisin bpn' (EC 3.4.21.62) | protein | 266 | 32% helix, 20% strand | P00782 |
Ligands and binding sites
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 | 94 | 0.38 | 0.76 | 27 | DFP |
Modifications
Observed in the structure: 1 covalent, 1 disulfide (covalent ligand, disulfide).
Compared structures
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 P00782
- Elsewhere: RCSB PDB 1SUE · PDBe 1SUE · UniProt P00782
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.