Research workbench
Crystal structure of aspergillus fumigatus chitinase B1 in complex with pentoxifylline
Analyse Crystal structure of aspergillus fumigatus chitinase B1 in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2A3C
- Type
- protein
- Length
- 789 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chitinase
- EC
- 3.2.1.14
- UniProt
- Q873X9
- Ligands
- PNX, SO4
- Pockets
- 6 · best druggability 0.62
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chitinase (EC 3.2.1.14) | protein | 395 | 37% helix, 20% strand | Q873X9 |
| B | Chitinase (EC 3.2.1.14) | protein | 394 | 38% helix, 20% strand | Q873X9 |
Ligands and binding sites
- PNX · 3,7-dimethyl-1-(5-oxohexyl)-3,7-dihydro-1H-purine-2,6-dione · ligand · 4 copies · chains A, B
- SO4 · Sulfate ion · ion · 7 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 177 | 0.62 | 0.83 | 31 | PNX |
| 2 | 170 | 0.61 | 0.83 | 32 | PNX |
| 3 | 203 | 0.50 | 0.76 | 34 | empty |
| 4 | 159 | 0.48 | 0.77 | 18 | PNX |
| 5 | 153 | 0.46 | 0.76 | 20 | PNX |
Interfaces
1 interface between chains.
- A–B · 433 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 2A3C · Crystal structure of Aspergillus fumigatus chitinase B1 in complex with pentoxifylline · the same entry in another collection · chain A against A, TM-score 1.00
- Q873X9 · AlphaFold monomer V2.0 prediction for endochitinase B1 (Q873X9) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 Q873X9
- Elsewhere: RCSB PDB 2A3C · PDBe 2A3C · UniProt Q873X9
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