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Crystal structure of mh-K1 chitosanase in substrate-bound form
Analyse Crystal structure of mh-K1 chitosanase in substrate-bound form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5HWA
- Type
- protein
- Length
- 259 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chitosanase
- EC
- 3.2.1.132
- UniProt
- P33673
- Ligands
- GCS, ZN
- Pockets
- 2 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 55% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chitosanase (EC 3.2.1.132) | protein | 259 | 55% helix, 6% strand | P33673 |
Ligands and binding sites
- GCS · 2-amino-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A
- ZN · Zinc ion · metal · 7 copies · chains A
- ACY · Acetic acid · additive · 3 copies · chains A
- CAC · Cacodylate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 284 | 0.57 | 0.78 | 43 | GCS |
| 2 | 83 | 0.42 | 0.79 | 17 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 P33673
- Elsewhere: RCSB PDB 5HWA · PDBe 5HWA · UniProt P33673
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