Research workbench
Crystal structure of HyHEL-10 Fv
Analyse Crystal structure of HyHEL-10 Fv in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5AYU
- Type
- protein
- Length
- 220 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.8
- Source
- Mus musculus
- Molecule
- lysozyme binding Ig kappa chain V23-J2 region; Ig VH,anti-lysozyme
Structure
x-ray diffraction · resolution 1.8 · 2 distinct chains · 5% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L | lysozyme binding Ig kappa chain V23-J2 region | protein | 107 | 3% helix, 50% strand | — |
| H | Ig VH,anti-lysozyme | protein | 113 | 8% helix, 51% strand | — |
Ligands and binding sites
- GOL · Glycerol · additive · 4 copies · chains L, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- L–H · 783 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 5AYU · Crystal structure of hyhel-10 fv · the same entry in another collection · chain H against H, 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 5AYU · PDBe 5AYU
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