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The crystal structure of the inactive form chitosanase from bacillus sp. K17 at PH3.7
Analyse The crystal structure of the inactive form chitosanase from bacillus sp. K17 at… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1V5C
- Type
- protein
- Length
- 386 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chitosanase
- EC
- 3.2.1.132
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chitosanase (EC 3.2.1.132) | protein | 386 | 50% helix, 6% strand | — |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 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 | 376 | 0.60 | 0.76 | 29 | empty |
Compared structures
- 1V5C · The crystal structure of the inactive form chitosanase from Bacillus sp. K17 at pH3.7 · 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
- Elsewhere: RCSB PDB 1V5C · PDBe 1V5C
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