Research workbench
Crystal structure of a family gh-19 chitinase from rye seeds
Analyse Crystal structure of a family gh-19 chitinase from rye seeds in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4DWX
- Type
- protein
- Length
- 484 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Basic endochitinase C
- EC
- 3.2.1.14
- UniProt
- Q9FRV0
- Ligands
- ZN, SO4
- Pockets
- 1 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Basic endochitinase C (EC 3.2.1.14) | protein | 242 | 45% helix, 2% strand | Q9FRV0 |
Ligands and binding sites
- ZN · Zinc ion · metal · 5 copies · chains A, B
- SO4 · Sulfate ion · ion · 3 copies · chains A, B
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 2 copies · chains A, B
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 | 937 | 0.82 | 0.84 | 77 | SO4, MES |
Interfaces
1 interface between chains.
- A–B · 586 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 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 Q9FRV0
- Elsewhere: RCSB PDB 4DWX · PDBe 4DWX · UniProt Q9FRV0
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