MolNFT v1 · #38334 · protein
Crystal structure of an aspartoacylase from rattus norvegicus
2GU2 · Aspa protein: “Crystal structure of an aspartoacylase from rattus norvegicus”. X-ray diffraction, 2 ligands (ZN, SO4), 6 pockets (best druggability 0.75). MolNFT v1 #38334 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 2GU2
- Type
- protein
- Length
- 614 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aspa protein
- EC
- 3.5.1.15
- UniProt
- Q9R1T5
- Ligands
- ZN, SO4
- Pockets
- 6 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Aspa protein (EC 3.5.1.15) | protein | 307 | 28% helix, 27% strand | Q9R1T5 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 909 | 0.75 | 0.79 | 70 | SO4 |
| 2 | 278 | 0.72 | 0.86 | 30 | ZN, SO4 |
| 3 | 251 | 0.71 | 0.86 | 32 | ZN |
| 4 | 153 | 0.50 | 0.79 | 29 | empty |
| 5 | 58 | 0.40 | 0.81 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1236 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 14 modified (engineered).
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 Q9R1T5
- Elsewhere: RCSB PDB 2GU2 · PDBe 2GU2 · UniProt Q9R1T5
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