Research workbench
Asparaginase from erwinia chrysanthemi, hexagonal form with sulfate
Analyse Asparaginase from erwinia chrysanthemi, hexagonal form with sulfate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HFJ
- Type
- protein
- Length
- 650 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-asparagine amidohydrolase
- EC
- 3.5.1.1
- UniProt
- P06608
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | L-asparagine amidohydrolase (EC 3.5.1.1) | protein | 325 | 32% helix, 22% strand | P06608 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 115 | 0.74 | 0.95 | 32 | empty |
| 2 | 245 | 0.66 | 0.84 | 38 | SO4 |
| 3 | 235 | 0.65 | 0.83 | 35 | SO4 |
Interfaces
1 interface between chains.
- A–C · 2406 Ų buried · 42 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 P06608
- Elsewhere: RCSB PDB 1HFJ · PDBe 1HFJ · UniProt P06608
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