MolNFT v1 · #102675 · protein
Structure of fully-cleaved glycine-bound human L-asparaginase protein
4OSY · Isoaspartyl PEPTIDASE/L-asparaginase: “Structure of fully-cleaved glycine-bound human L-asparaginase protein”. X-ray diffraction, 2 ligands (GLY, NA), 3 pockets (best druggability 0.56). MolNFT v1 #102675 on GenesisL1: 3D structure…
- PDB
- 4OSY
- Type
- protein
- Length
- 590 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Isoaspartyl PEPTIDASE/L-asparaginase
- EC
- 3.4.19.5, 3.5.1.1
- UniProt
- Q7L266
- Ligands
- GLY, NA
- Pockets
- 3 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Isoaspartyl PEPTIDASE/L-asparaginase (EC 3.4.19.5, 3.5.1.1) | protein | 295 | 35% helix, 25% strand | Q7L266 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 231 | 0.56 | 0.78 | 36 | GLY |
| 2 | 216 | 0.56 | 0.79 | 36 | GLY |
| 3 | 113 | 0.38 | 0.74 | 27 | empty |
Interfaces
1 interface between chains.
- A–B · 1851 Ų buried · 27 hydrogen bonds · protein-protein
Compared structures
- 4OSY · STRUCTURE of FULLY-CLEAVED GLYCINE-BOUND HUMAN L-ASPARAGINASE PROTEIN · the same entry in another collection · chain A against A, TM-score 1.00
- Q7L266 · AlphaFold monomer V2.0 prediction for isoaspartyl PEPTIDASE/L-asparaginase (Q7L266) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 Q7L266
- Elsewhere: RCSB PDB 4OSY · PDBe 4OSY · UniProt Q7L266
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