Research workbench
Structure of hexagonal turkey egg white lysozyme at 1.65 ångströms resolution
Analyse Structure of hexagonal turkey egg white lysozyme at 1.65 ångströms resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TEW
- Type
- protein
- Length
- 128 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Turkey egg white lysozyme
- EC
- 3.2.1.17
- UniProt
- P00703
- Ligands
- SCN
- Pockets
- 1 · best druggability 0.33
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Turkey egg white lysozyme (EC 3.2.1.17) | protein | 128 | 43% helix, 9% strand | P00703 |
Ligands and binding sites
- SCN · Thiocyanate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 51 | 0.33 | 0.78 | 13 | empty |
Modifications
Observed in the structure: 4 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 P00703
- Elsewhere: RCSB PDB 1TEW · PDBe 1TEW · UniProt P00703
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