Research workbench
Class IV chitinase structure from picea abies at 1.55A
Analyse Class IV chitinase structure from picea abies at 1.55A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3HBE
- Type
- protein
- Length
- 204 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Class IV chitinase CHIA4-PA2
- EC
- 3.2.1.14
- UniProt
- Q6WSR8
- Ligands
- FOR
- Pockets
- 1 · best druggability 0.37
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Class IV chitinase CHIA4-PA2 (EC 3.2.1.14) | protein | 204 | 52% helix, 1% strand | Q6WSR8 |
Ligands and binding sites
- FOR · Formyl group · ligand · chains X
- MXE · 2-methoxyethanol · additive · chains X
- ACT · Acetate ion · additive · chains X
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 96 | 0.37 | 0.75 | 20 | MXE, ACT, FOR |
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 3HBE · Class IV chitinase structure from Picea abies at 1.55A · the same entry in another collection · chain X against X, 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
- Every structure of UniProt Q6WSR8
- Elsewhere: RCSB PDB 3HBE · PDBe 3HBE · UniProt Q6WSR8
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