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Crystal structure of apo-aspartoacylase from human brain
Analyse Crystal structure of apo-aspartoacylase from human brain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2O53
- Type
- protein
- Length
- 604 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aspartoacylase
- EC
- 3.5.1.15
- UniProt
- P45381
- Ligands
- ZN, PO4
- Pockets
- 5 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Aspartoacylase (EC 3.5.1.15) | protein | 302 | 27% helix, 27% strand | P45381 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 81 | 0.74 | 0.97 | 21 | ZN, PO4 |
| 2 | 828 | 0.73 | 0.78 | 60 | empty |
| 3 | 123 | 0.70 | 0.91 | 28 | ZN, PO4 |
| 4 | 117 | 0.44 | 0.78 | 21 | empty |
| 5 | 73 | 0.34 | 0.76 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 1233 Ų buried · 16 hydrogen bonds · protein-protein
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 P45381
- Elsewhere: RCSB PDB 2O53 · PDBe 2O53 · UniProt P45381
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