Research workbench
Cartilage homing cysteine-dense-peptides
Analyse Cartilage homing cysteine-dense-peptides in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6AY7
- Type
- protein
- Length
- 78 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.77
- Source
- Androctonus australis
- Molecule
- Potassium channel toxin alpha-KTx 3.5
- UniProt
- P45696
- Ligands
- SO4, CL
Structure
x-ray diffraction · resolution 1.77 · 1 distinct chain · 26% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Potassium channel toxin alpha-KTx 3.5 | protein | 39 | 26% helix, 44% strand | P45696 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains A, B
- CL · Chloride ion · ion · 2 copies · chains A, B
- TFA · trifluoroacetic acid · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 323 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
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 P45696
- Elsewhere: RCSB PDB 6AY7 · PDBe 6AY7 · UniProt P45696
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