Research workbench
Crystal structure of chitinase C mutant E147Q
Analyse Crystal structure of chitinase C mutant E147Q in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1WVV
- Type
- protein
- Length
- 462 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chitinase C
- EC
- 3.2.1.14
- Ligands
- CL
- Pockets
- 3 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chitinase C (EC 3.2.1.14) | protein | 209 | 52% helix, 1% strand | — |
| B | Chitinase C (EC 3.2.1.14) | protein | 253 | 43% helix, 9% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 201 | 0.68 | 0.86 | 37 | CL |
| 2 | 245 | 0.67 | 0.84 | 33 | GOL |
| 3 | 393 | 0.62 | 0.77 | 41 | CL, GOL |
Interfaces
1 interface between chains.
- A–B · 1057 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 1WVV · Crystal structure of chitinase C mutant E147Q · 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 1WVV · PDBe 1WVV
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