Research workbench
NMR study of the proline repeat from tus
Analyse NMR study of the proline repeat from tus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SUT
- Type
- protein
- Length
- 22 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tus proline repeat
- UniProt
- P16525
Structure
solution nmr · 1 distinct chain · 23% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tus proline repeat | protein | 22 | 23% helix, 18% strand | P16525 |
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 P16525
- Elsewhere: RCSB PDB 1SUT · PDBe 1SUT · UniProt P16525
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