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Crystal structure of sulfate-bound human l-asparaginase protein

Analyse Crystal structure of sulfate-bound human l-asparaginase protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4PVQ
Type
protein
Length
590 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.13
Source
Homo sapiens
Molecule
Isoaspartyl peptidase/L-asparaginase
EC
3.4.19.5, 3.5.1.1
UniProt
Q7L266
Ligands
NA, SO4, IOD
Pockets
4 · best druggability 0.57

Structure

x-ray diffraction · resolution 2.13 · 2 distinct chains · 35% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AIsoaspartyl peptidase/L-asparaginase (EC 3.4.19.5, 3.5.1.1)protein29435% helix, 27% strandQ7L266
BIsoaspartyl peptidase/L-asparaginase (EC 3.4.19.5, 3.5.1.1)protein29635% helix, 26% strandQ7L266

Ligands and binding sites

  • NA · Sodium ion · metal · 2 copies · chains A, B
  • SO4 · Sulfate ion · ion · 13 copies · chains A, B
  • IOD · Iodide ion · ion · 4 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11550.570.8225empty
21270.470.7929SO4
3870.400.7827SO4
4570.280.7413empty

Interfaces

1 interface between chains.

  • A–B · 1874 Ų buried · 36 hydrogen bonds · protein-protein

Compared structures

  • 4PVQ · Crystal structure of sulfate-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 A against A, TM-score 0.99

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