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Determination of the three-dimensional solution structure of the antihypertensive and antiviral protein bds-I from the sea anemone anemonia sulcata. a study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing
Analyse Determination of the three-dimensional solution structure of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BDS
- Type
- protein
- Length
- 43 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bds-I
- UniProt
- P11494
Structure
solution nmr · 1 distinct chain · 0% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bds-I | protein | 43 | 0% helix, 26% strand | P11494 |
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 1BDS · Determination of the three-dimensional solution structure of the antihypertensive and… · the same entry in another collection · chain A against A, TM-score 1.00
- P11494 · AlphaFold monomer V2.0 prediction for DELTA/KAPPA-actitoxin-AVD4A (P11494) · a predicted model of the same protein · chain A against A, TM-score 0.69
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 P11494
- Elsewhere: RCSB PDB 1BDS · PDBe 1BDS · UniProt P11494
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