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Asparaginase from E. COLI, mutant T89V with covalently bound aspartate

Analyse Asparaginase from E. COLI, mutant T89V with covalently bound aspartate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4ECA
Type
protein
Length
1,304 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
L-asparagine amidohydrolase
EC
3.5.1.1
UniProt
P00805
Pockets
11 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DL-asparagine amidohydrolase (EC 3.5.1.1)protein32634% helix, 24% strandP00805

Pockets

11 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12150.810.9554empty
21940.790.9452empty
31640.780.9543empty
41200.770.9629empty
5800.710.9530empty

Interfaces

6 interfaces between chains.

  • A–C · 2408 Ų buried · 56 hydrogen bonds · protein-protein
  • B–D · 2407 Ų buried · 55 hydrogen bonds · protein-protein
  • A–D · 1057 Ų buried · 23 hydrogen bonds · protein-protein
  • B–C · 1039 Ų buried · 23 hydrogen bonds · protein-protein
  • A–B · 1029 Ų buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide, 4 modified (disulfide, nonstandard).

Compared structures

  • 4ECA · Asparaginase from E. COLI, mutant T89V with covalently bound aspartate · the same entry in another collection · chain D against D, TM-score 1.00
  • P00805 · AlphaFold monomer V2.0 prediction for L-asparaginase 2 (P00805) · a predicted model of the same protein · chain A against A, TM-score 1.00

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