Research workbench
Subtilisin-carlsberg complexed with xenon (8 bar)
Analyse Subtilisin-carlsberg complexed with xenon (8 bar) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1C3L
- Type
- protein
- Length
- 274 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Subtilisin-carlsberg
- EC
- 3.4.21.62
- UniProt
- P00780
- Ligands
- CA, XE
- Pockets
- 1 · best druggability 0.35
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Subtilisin-carlsberg (EC 3.4.21.62) | protein | 274 | 30% helix, 20% strand | P00780 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains A
- XE · Xenon · ion · chains A
- FMT · Formic acid · additive · 3 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 | 87 | 0.35 | 0.75 | 32 | XE, FMT |
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 P00780
- Elsewhere: RCSB PDB 1C3L · PDBe 1C3L · UniProt P00780
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