Research workbench
Alpha-bungarotoxin complexed with high affinity peptide
Analyse Alpha-bungarotoxin complexed with high affinity peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HC9
- Type
- protein
- Length
- 173 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-bungarotoxin isoform V31; Alpha-bungarotoxin isoform A31; Peptide inhibitor
- UniProt
- P60616, P60615
- Ligands
- IOD
Structure
x-ray diffraction · 4 distinct chains · 5% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-bungarotoxin isoform V31 | protein | 74 | 5% helix, 36% strand | P60616 |
| B | Alpha-bungarotoxin isoform A31 | protein | 74 | 5% helix, 36% strand | P60615 |
| C | Peptide inhibitor | protein | 13 | 0% helix, 62% strand | — |
| D | Peptide inhibitor | protein | 12 | 0% helix, 17% strand | — |
Ligands and binding sites
- IOD · Iodide ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
2 interfaces between chains.
- B–D · 672 Ų buried · 15 hydrogen bonds · protein-protein
- A–C · 670 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 disulfide (disulfide).
Compared structures
- 1HC9 · alpha-bungarotoxin complexed with high affinity peptide · the same entry in another collection · chain A against A, TM-score 1.00
- P60616 · AlphaFold monomer V2.0 prediction for alpha-bungarotoxin isoform V31 (P60616) · a predicted model of the same protein · chain A against A, TM-score 0.98
- P60615 · AlphaFold monomer V2.0 prediction for alpha-bungarotoxin (P60615) · a predicted model of the same protein · chain B against A, TM-score 0.97
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 P60616
- Every structure of UniProt P60615
- Elsewhere: RCSB PDB 1HC9 · PDBe 1HC9 · UniProt P60616 · UniProt P60615
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