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CIS/TRANS isomerization of non-prolyl peptide bond observed in crystal structure of an scorpion toxin
Analyse CIS/TRANS isomerization of non-prolyl peptide bond observed in crystal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1KV0
- Type
- protein
- Length
- 132 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-like toxin bmk-M7
- UniProt
- P59854
Structure
x-ray diffraction · 1 distinct chain · 15% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Alpha-like toxin bmk-M7 | protein | 66 | 15% helix, 38% strand | P59854 |
Interfaces
1 interface between chains.
- A–B · 476 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
- 1KV0 · Cis/trans Isomerization of Non-prolyl Peptide Bond Observed in Crystal Structure of an… · the same entry in another collection · chain A against A, TM-score 1.00
- P59854 · AlphaFold monomer V2.0 prediction for alpha-like toxin bmk-M7 (P59854) · a predicted model of the same protein · chain A against A, TM-score 0.91
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 P59854
- Elsewhere: RCSB PDB 1KV0 · PDBe 1KV0 · UniProt P59854
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