Research workbench
Three-dimensional structure of the two peptides that constitute the two-peptide bacteriocin plantaracin ef
Analyse Three-dimensional structure of the two peptides that constitute the two-peptide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2RLW
- Type
- protein
- Length
- 34 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Plnf
- UniProt
- P71469
Structure
solution nmr · 1 distinct chain · 76% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Plnf | protein | 34 | 76% helix, 0% strand | P71469 |
Compared structures
- 2RLW · Three-Dimensional Structure of the two Peptides that Constitute the Two-Peptide… · the same entry in another collection · chain A against A, TM-score 1.00
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 P71469
- Elsewhere: RCSB PDB 2RLW · PDBe 2RLW · UniProt P71469
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