MolNFT v1 · #166391 · protein
Asparaginase II from escherichia COLI
6UOH · L-asparaginase 2: “Asparaginase II from escherichia COLI”. X-ray diffraction, 1 ligand (ASP), 2 pockets (best druggability 0.62). MolNFT v1 #166391 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6UOH
- Type
- protein
- Length
- 652 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-asparaginase 2
- EC
- 3.5.1.1
- UniProt
- A0A377K0N3
- Ligands
- ASP
- Pockets
- 2 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | L-asparaginase 2 (EC 3.5.1.1) | protein | 326 | 34% helix, 22% strand | A0A377K0N3 |
Ligands and binding sites
- ASP · Aspartic acid · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 394 | 0.62 | 0.77 | 55 | empty |
| 2 | 239 | 0.56 | 0.79 | 30 | empty |
Interfaces
1 interface between chains.
- A–B · 1041 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 6UOH · Asparaginase II from Escherichia coli · the same entry in another collection · chain A against A, 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 A0A377K0N3
- Elsewhere: RCSB PDB 6UOH · PDBe 6UOH · UniProt A0A377K0N3
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.