Research workbench
Human lysozyme mutant A96L
Analyse Human lysozyme mutant A96L in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BB3
- Type
- protein
- Length
- 260 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lysozyme
- EC
- 3.2.1.17
- UniProt
- P61626
- Pockets
- 3 · best druggability 0.46
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Lysozyme (EC 3.2.1.17) | protein | 130 | 42% helix, 11% strand | P61626 |
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 | 133 | 0.46 | 0.77 | 19 | empty |
| 2 | 147 | 0.43 | 0.75 | 25 | empty |
| 3 | 63 | 0.31 | 0.75 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 553 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
- 1BB3 · Human lysozyme mutant A96L · 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 P61626
- Elsewhere: RCSB PDB 1BB3 · PDBe 1BB3 · UniProt P61626
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