Research workbench
Subtilisin dy in complex with the synthetic inhibitor N- benzyloxycarbonyl-ala-pro-phe-chloromethyl ketone
Analyse Subtilisin dy in complex with the synthetic inhibitor N… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BH6
- Type
- protein
- Length
- 274 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Subtilisin dy
- EC
- 3.4.21.62
- UniProt
- P00781
- Ligands
- 1BH, CA, NA
- Pockets
- 1 · best druggability 0.44
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Subtilisin dy (EC 3.4.21.62) | protein | 274 | 30% helix, 20% strand | P00781 |
Ligands and binding sites
- 1BH · N-benzyloxycarbonyl-ala-pro-3-amino-4-phenyl-butan-2-ol · ligand · chains A
- CA · Calcium ion · metal · chains A
- NA · Sodium ion · metal · 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 | 142 | 0.44 | 0.76 | 36 | 1BH |
Modifications
Observed in the structure: 2 covalent (covalent ligand).
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 P00781
- Elsewhere: RCSB PDB 1BH6 · PDBe 1BH6 · UniProt P00781
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