Research workbench
The NMR solution structure of the peptide AC12 from hypsiboas raniceps
Analyse The NMR solution structure of the peptide AC12 from hypsiboas raniceps in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FGM
- Type
- protein
- Length
- 12 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ala-cys-phe-leu-thr-arg-leu-gly-thr-tyr-val-cys
Structure
solution nmr · 1 distinct chain · 0% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ala-cys-phe-leu-thr-arg-leu-gly-thr-tyr-val-cys | protein | 12 | 0% helix, 33% strand | — |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 6FGM · The NMR solution structure of the peptide AC12 from Hypsiboas raniceps · 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
- Elsewhere: RCSB PDB 6FGM · PDBe 6FGM
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