Research workbench
Xray crystal structure of lysozyme mutant L20/R63A liganded to ethylguanidinium
Analyse Xray crystal structure of lysozyme mutant L20/R63A liganded to ethylguanidinium in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2F32
- Type
- protein
- Length
- 175 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lysozyme
- EC
- 3.2.1.17
- UniProt
- P00720
- Ligands
- EGD
- Pockets
- 2 · best druggability 0.44
Structure
x-ray diffraction · 1 distinct chain · 64% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lysozyme (EC 3.2.1.17) | protein | 175 | 64% helix, 10% 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 142 | 0.44 | 0.76 | 20 | empty |
| 2 | 77 | 0.31 | 0.73 | 14 | empty |
Compared structures
- 2F32 · Xray crystal structure of lysozyme mutant L20/R63A liganded to ethylguanidinium · 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 2F32 · PDBe 2F32 · UniProt P00720
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