MolNFT v1 · #101851 · protein
Crystal structure of cleaved guinea pig L-asparaginase type III in complex with L-aspartate
4O48 · Uncharacterized protein: “Crystal structure of cleaved guinea pig L-asparaginase type III in complex with L-aspartate”. X-ray diffraction, 2 ligands (ASP, NA), 5 pockets (best druggability 0.63). MolNFT v1 #101851 on GenesisL1: 3D…
- PDB
- 4O48
- Type
- protein
- Length
- 596 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein
- EC
- 3.5.1.1
- UniProt
- H0VQC8
- Ligands
- ASP, NA
- Pockets
- 5 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Uncharacterized protein (EC 3.5.1.1) | protein | 298 | 36% helix, 26% strand | H0VQC8 |
Ligands and binding sites
- ASP · Aspartic acid · ligand · 2 copies · chains A, B
- NA · Sodium ion · metal · 2 copies · chains A, B
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 | 338 | 0.63 | 0.79 | 42 | ASP |
| 2 | 366 | 0.62 | 0.78 | 42 | ASP |
| 3 | 192 | 0.52 | 0.78 | 31 | empty |
| 4 | 114 | 0.43 | 0.77 | 27 | empty |
| 5 | 54 | 0.25 | 0.73 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 1758 Ų buried · 21 hydrogen bonds · protein-protein
Compared structures
- 4O48 · Crystal structure of cleaved guinea pig L-asparaginase type III in complex with… · the same entry in another collection · chain B against B, TM-score 1.00
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 H0VQC8
- Elsewhere: RCSB PDB 4O48 · PDBe 4O48 · UniProt H0VQC8
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