Research workbench
Structure of disulfide bond deletion mutant of ostrich egg white lysozyme
Analyse Structure of disulfide bond deletion mutant of ostrich egg white lysozyme in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WYH
- Type
- protein
- Length
- 370 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lysozyme G
- EC
- 3.2.1.17
- UniProt
- P00719
- Ligands
- TAM
- Pockets
- 3 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 55% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Lysozyme G (EC 3.2.1.17) | protein | 185 | 55% helix, 6% strand | P00719 |
Ligands and binding sites
- TAM · Tris(hydroxyethyl)aminomethane · ligand · 2 copies · chains A, B
- P6G · Hexaethylene glycol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 195 | 0.50 | 0.77 | 34 | TAM, P6G |
| 2 | 185 | 0.46 | 0.75 | 35 | TAM |
| 3 | 89 | 0.40 | 0.78 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 622 Ų buried · 4 hydrogen bonds · protein-protein
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 P00719
- Elsewhere: RCSB PDB 3WYH · PDBe 3WYH · UniProt P00719
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