Research workbench
Cu-mediated dimer of T4 lysozyme R76H/R80H by synthetic symmetrization
Analyse Cu-mediated dimer of T4 lysozyme R76H/R80H by synthetic symmetrization in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3SB9
- Type
- protein
- Length
- 326 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lysozyme
- EC
- 3.2.1.17
- UniProt
- P00720
- Ligands
- CU
- Pockets
- 2 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 64% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Lysozyme (EC 3.2.1.17) | protein | 163 | 64% helix, 9% strand | P00720 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 319 | 0.84 | 0.93 | 37 | empty |
| 2 | 168 | 0.41 | 0.73 | 27 | empty |
Interfaces
1 interface between chains.
- A–B · 905 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 3SB9 · Cu-mediated Dimer of T4 Lysozyme R76H/R80H by Synthetic Symmetrization · the same entry in another collection · chain A against A, 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 P00720
- Elsewhere: RCSB PDB 3SB9 · PDBe 3SB9 · UniProt P00720
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.