Research workbench
A comparison of the three-dimensional structures of subtilisin bpn and subtilisin novo
Analyse A comparison of the three-dimensional structures of subtilisin bpn and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2SBT
- Type
- protein
- Length
- 275 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Subtilisin novo
- EC
- 3.4.21.14
- UniProt
- P00782
- Ligands
- ACN
- Pockets
- 2 · best druggability 0.43
Structure
x-ray diffraction · 1 distinct chain · 21% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Subtilisin novo (EC 3.4.21.14) | protein | 275 | 21% helix, 14% strand | P00782 |
Ligands and binding sites
- ACN · Acetone · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 153 | 0.43 | 0.75 | 35 | empty |
| 2 | 56 | 0.29 | 0.75 | 15 | empty |
Compared structures
- 2SBT · A comparison of the three-dimensional structures of subtilisin bpn and subtilisin novo · the same entry in another collection · 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 P00782
- Elsewhere: RCSB PDB 2SBT · PDBe 2SBT · UniProt P00782
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