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L-asparaginase from erwinia carotovora in complex with aspartic acid

Analyse L-asparaginase from erwinia carotovora in complex with aspartic acid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2GVN
Type
protein
Length
2,600 residues
Chains
8
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
L-asparaginase
EC
3.5.1.1
Ligands
ASP
Pockets
20 · best druggability 0.89

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, HL-asparaginase (EC 3.5.1.1)protein32531% helix, 20% strand—

Ligands and binding sites

  • ASP · Aspartic acid · ligand · 8 copies · chains A, E, B, F, C, G, D, H

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

Pockets

20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19550.890.92134empty
29330.890.92128empty
310950.790.8198ASP
43620.740.8659ASP
53810.740.8557ASP

Interfaces

15 interfaces between chains.

  • C–G · 2323 Ų buried · 47 hydrogen bonds · protein-protein
  • B–F · 2321 Ų buried · 46 hydrogen bonds · protein-protein
  • D–H · 2312 Ų buried · 45 hydrogen bonds · protein-protein
  • A–E · 2300 Ų buried · 47 hydrogen bonds · protein-protein
  • D–G · 1142 Ų buried · 23 hydrogen bonds · protein-protein

Compared structures

  • 2GVN · L-asparaginase from Erwinia carotovora in complex with aspartic acid · the same entry in another collection · chain H against H, TM-score 1.00

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