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Crystal structure of the Asn-bound guinea pig L-asparaginase 1 catalytic domain active site mutant T19A

Analyse Crystal structure of the Asn-bound guinea pig L-asparaginase 1 catalytic domain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5DNC
Type
protein
Length
1,419 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.01
Source
Cavia porcellus
Molecule
L-asparaginase
UniProt
H0W0T5
Ligands
ASN
Pockets
20 · best druggability 0.85

Structure

x-ray diffraction · resolution 2.01 · 3 distinct chains · 29% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CL-asparaginaseprotein35429% helix, 25% strandH0W0T5
BL-asparaginaseprotein35528% helix, 25% strandH0W0T5
DL-asparaginaseprotein35629% helix, 25% strandH0W0T5

Ligands and binding sites

  • ASN · Asparagine · ligand · 4 copies · chains A, D, B, C
  • EDO · 1,2-ethanediol · additive · 17 copies · chains A, B, C, D

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

Pockets

20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14650.850.9295EDO
24810.850.91102EDO
31250.760.9523empty
41340.760.9419empty
52570.630.8144ASN

Interfaces

5 interfaces between chains.

  • B–C · 2109 Ų buried · 35 hydrogen bonds · protein-protein
  • A–D · 2076 Ų buried · 40 hydrogen bonds · protein-protein
  • C–D · 1182 Ų buried · 7 hydrogen bonds · protein-protein
  • A–B · 1136 Ų buried · 6 hydrogen bonds · protein-protein
  • A–C · 19 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 5DNC · Crystal structure of the asn-bound guinea pig L-asparaginase 1 catalytic domain active… · the same entry in another collection · chain A against A, TM-score 1.00

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