Research workbench
Nisin cyclase
Analyse Nisin cyclase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2G0D
- Type
- protein
- Length
- 404 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nisin biosynthesis protein nisc
- UniProt
- Q03202
- Ligands
- ZN
- Pockets
- 4 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 61% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nisin biosynthesis protein nisc | protein | 404 | 61% helix, 1% strand | Q03202 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 133 | 0.50 | 0.79 | 20 | empty |
| 2 | 51 | 0.37 | 0.79 | 14 | empty |
| 3 | 85 | 0.36 | 0.75 | 24 | empty |
| 4 | 64 | 0.34 | 0.77 | 15 | empty |
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 Q03202
- Elsewhere: RCSB PDB 2G0D · PDBe 2G0D · UniProt Q03202
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