Research workbench
Insect chitin deacetylase
Analyse Insect chitin deacetylase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ZNS
- Type
- protein
- Length
- 381 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chitin deacetylase
- UniProt
- H9J9M0
- Ligands
- NAG, ZN
- Pockets
- 3 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chitin deacetylase | protein | 381 | 31% helix, 15% strand | H9J9M0 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A
- ZN · Zinc ion · metal · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 188 | 0.58 | 0.81 | 28 | NAG |
| 2 | 106 | 0.45 | 0.79 | 17 | empty |
| 3 | 102 | 0.37 | 0.75 | 25 | empty |
Modifications
Observed in the structure: 11 modified, 7 disulfide, 2 glycan (engineered, disulfide, N-glycosylation).
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 H9J9M0
- Elsewhere: RCSB PDB 5ZNS · PDBe 5ZNS · UniProt H9J9M0
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