Research workbench
Ni(II)-substituted Wells-Dawson binding to Hen Egg-White Lysozyme (HEWL)
Analyse Ni(II)-substituted Wells-Dawson binding to Hen Egg-White Lysozyme (HEWL) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HY6
- Type
- protein
- Length
- 128 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.87
- Source
- Gallus gallus
- Molecule
- Lysozyme C
- EC
- 3.2.1.17
- UniProt
- P00698
- Ligands
- GXZ, CL
Structure
x-ray diffraction · resolution 1.87 · 1 distinct chain · 41% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Lysozyme C (EC 3.2.1.17) | protein | 128 | 41% helix, 11% strand | P00698 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 6HY6 · NI(II)-substituted wells-dawson binding to hen egg-white lysozyme (hewl) · the same entry in another collection · chain B against B, 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
- Every structure of UniProt P00698
- Elsewhere: RCSB PDB 6HY6 · PDBe 6HY6 · UniProt P00698
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