MolNFT v1 · #166387 · protein
Asparaginase II from escherichia COLI
6UOD · L-asparaginase 2: “Asparaginase II from escherichia COLI”. X-ray diffraction, 17 pockets (best druggability 0.67). MolNFT v1 #166387 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6UOD
- Type
- protein
- Length
- 1,240 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-asparaginase 2
- EC
- 3.5.1.1
- UniProt
- A0A376KNM9
- Pockets
- 17 · best druggability 0.67
Structure
x-ray diffraction · 4 distinct chains · 33% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | L-asparaginase 2 (EC 3.5.1.1) | protein | 311 | 32% helix, 22% strand | A0A376KNM9 |
| B | L-asparaginase 2 (EC 3.5.1.1) | protein | 309 | 34% helix, 22% strand | A0A376KNM9 |
| C | L-asparaginase 2 (EC 3.5.1.1) | protein | 312 | 34% helix, 21% strand | A0A376KNM9 |
| D | L-asparaginase 2 (EC 3.5.1.1) | protein | 308 | 33% helix, 21% strand | A0A376KNM9 |
Pockets
17 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 123 | 0.67 | 0.90 | 31 | empty |
| 2 | 280 | 0.62 | 0.80 | 37 | empty |
| 3 | 121 | 0.60 | 0.86 | 18 | empty |
| 4 | 299 | 0.56 | 0.77 | 28 | empty |
| 5 | 336 | 0.56 | 0.76 | 32 | empty |
Interfaces
4 interfaces between chains.
- A–B · 2060 Ų buried · 37 hydrogen bonds · protein-protein
- C–D · 505 Ų buried · 2 hydrogen bonds · protein-protein
- A–D · 272 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 251 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 6UOD · 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 A0A376KNM9
- Elsewhere: RCSB PDB 6UOD · PDBe 6UOD · UniProt A0A376KNM9
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