Research workbench
Acidic mammalian chinase, catalytic domain
Analyse Acidic mammalian chinase, catalytic domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FXY
- Type
- protein
- Length
- 1,510 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acidic mammalian chitinase
- EC
- 3.2.1.14
- UniProt
- Q9BZP6
- Pockets
- 13 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, D | Acidic mammalian chitinase (EC 3.2.1.14) | protein | 379 | 38% helix, 22% strand | Q9BZP6 |
| B | Acidic mammalian chitinase (EC 3.2.1.14) | protein | 373 | 39% helix, 23% strand | Q9BZP6 |
Pockets
13 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 279 | 0.63 | 0.80 | 35 | empty |
| 2 | 690 | 0.63 | 0.73 | 55 | empty |
| 3 | 343 | 0.60 | 0.77 | 52 | empty |
| 4 | 358 | 0.59 | 0.76 | 42 | empty |
| 5 | 346 | 0.59 | 0.76 | 44 | empty |
Interfaces
4 interfaces between chains.
- A–B · 784 Ų buried · 10 hydrogen bonds · protein-protein
- B–C · 562 Ų buried · 5 hydrogen bonds · protein-protein
- B–D · 287 Ų buried · 1 hydrogen bond · protein-protein
- A–D · 147 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 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 Q9BZP6
- Elsewhere: RCSB PDB 3FXY · PDBe 3FXY · UniProt Q9BZP6
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