Research workbench
Solution NMR structure of peptidase domain from clostridium thermocellum PCAT1
Analyse Solution NMR structure of peptidase domain from clostridium thermocellum PCAT1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7N87
- Type
- protein
- Length
- 151 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ABC-type bacteriocin transporter
- UniProt
- A3DCU1
Structure
solution nmr · 1 distinct chain · 28% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ABC-type bacteriocin transporter | protein | 151 | 28% helix, 29% strand | A3DCU1 |
Compared structures
- 7N87 · Solution NMR structure of peptidase domain from Clostridium thermocellum PCAT1 · 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 A3DCU1
- Elsewhere: RCSB PDB 7N87 · PDBe 7N87 · UniProt A3DCU1
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