Research workbench
AlphaFold monomer V2.0 prediction for nisin biosynthesis protein nisb (P20103)
Analyse AlphaFold monomer V2.0 prediction for nisin biosynthesis protein nisb (P20103) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P20103
- Type
- protein
- Length
- 993 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xcFf9BA0aF3DBABCc89e611059882CCFef4E731f4
- Molecule
- Nisin biosynthesis protein nisb
- UniProt
- P20103
- Pockets
- 14 · best druggability 0.78
Structure
1 distinct chain · 46% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nisin biosynthesis protein nisb | protein | 993 | 46% helix, 21% strand | P20103 |
Pockets
14 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 933 | 0.78 | 0.80 | 90 | empty |
| 2 | 605 | 0.75 | 0.82 | 58 | empty |
| 3 | 900 | 0.73 | 0.77 | 70 | empty |
| 4 | 368 | 0.65 | 0.80 | 33 | empty |
| 5 | 194 | 0.52 | 0.77 | 28 | empty |
Compared structures
- 6M7Y · Dehydratase, NisB, bound to a non-eliminable substrate analog · an experimental structure of the same protein · chain A against B, TM-score 0.95
- 6M7Y · Dehydratase, nisb, bound to a non-eliminable substrate analog · an experimental structure of the same protein · chain A against B, TM-score 0.95
- 4WD9 · Crystal structure of tRNA-dependent lantibiotic dehydratase nisb in complex with nisa… · an experimental structure of the same protein · chain A against B, TM-score 0.95
- 4WD9 · Crystal structure of tRNA-dependent lantibiotic dehydratase NisB in complex with NisA… · an experimental structure of the same protein · chain A against B, TM-score 0.95
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 P20103
- Elsewhere: UniProt P20103 · AlphaFold DB P20103
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