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Crystal structure of murine aminoacylase 3
Analyse Crystal structure of murine aminoacylase 3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3NH4
- Type
- protein
- Length
- 303 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aspartoacylase-2
- EC
- 3.5.1.-
- UniProt
- Q91XE4
- Ligands
- CS, ZN, CL
- Pockets
- 3 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aspartoacylase-2 (EC 3.5.1.-) | protein | 303 | 27% helix, 27% strand | Q91XE4 |
Ligands and binding sites
- CS · Cesium ion · metal · 2 copies · chains A
- ZN · Zinc ion · metal · chains A
- CL · Chloride ion · ion · 2 copies · chains A
- ACT · Acetate ion · additive · chains A
- FMT · Formic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 158 | 0.71 | 0.90 | 26 | ACT, FMT |
| 2 | 62 | 0.30 | 0.74 | 14 | empty |
| 3 | 52 | 0.28 | 0.75 | 14 | empty |
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 Q91XE4
- Elsewhere: RCSB PDB 3NH4 · PDBe 3NH4 · UniProt Q91XE4
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