Research workbench
Bacillus lentus substilisin variant (ser 87) K27R/V104Y/N123S/T274A
Analyse Bacillus lentus substilisin variant (ser 87) K27R/V104Y/N123S/T274A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1C9N
- Type
- protein
- Length
- 269 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serine protease
- EC
- 3.4.21.62
- UniProt
- P29600
- Ligands
- CA, SO4
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serine protease (EC 3.4.21.62) | protein | 269 | 30% helix, 21% strand | P29600 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 modified (nonstandard).
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 P29600
- Elsewhere: RCSB PDB 1C9N · PDBe 1C9N · UniProt P29600
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