MolNFT v1 · #125 · protein
The refined structures of goose lysozyme and its complex with a bound trisaccharide show that the "goose-type lysozymes lack a catalytic aspartate
154L: “The refined structures of goose lysozyme and its complex with a bound trisaccharide show that the "goose-type…”. X-ray diffraction, 1 ligand (NAG), 1 pocket (best druggability 0.50). MolNFT v1 #125 on GenesisL1: 3D structure…
- PDB
- 154L
- Type
- protein
- Length
- 185 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Goose lysozyme
- EC
- 3.2.1.17
- UniProt
- P00718
- Ligands
- NAG
- Pockets
- 1 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 56% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Goose lysozyme (EC 3.2.1.17) | protein | 185 | 56% helix, 4% strand | P00718 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 246 | 0.50 | 0.75 | 32 | NAG |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 154L · The refined structures of goose lysozyme and its complex with a bound trisaccharide show… · the same entry in another collection · chain A against A, TM-score 1.00
- P00718 · AlphaFold monomer V2.0 prediction for lysozyme G (P00718) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P00718
- Elsewhere: RCSB PDB 154L · PDBe 154L · UniProt P00718
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