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MolNFT v1 · #102674 · protein

Structure of uncleaved glycine-bound human L-asparaginase protein

4OSX · Isoaspartyl PEPTIDASE/L-asparaginase: “Structure of uncleaved glycine-bound human L-asparaginase protein”. X-ray diffraction, 2 ligands (GLY, NA), 3 pockets (best druggability 0.57). MolNFT v1 #102674 on GenesisL1: 3D structure…

PDB
4OSX
Type
protein
Length
600 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 0.57

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BIsoaspartyl PEPTIDASE/L-asparaginase (EC 3.4.19.5, 3.5.1.1)protein30033% helix, 27% strandQ7L266

Ligands and binding sites

  • GLY · Glycine · ligand · 5 copies · chains A, B
  • NA · Sodium ion · metal · 2 copies · chains A, B

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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11970.570.8041GLY
21530.510.7931GLY
3950.380.7624empty

Interfaces

1 interface between chains.

  • A–B · 1896 Ų buried · 32 hydrogen bonds · protein-protein

Compared structures

  • 4OSX · STRUCTURE of UNCLEAVED 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

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