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Crystal structure of asparaginyl endopeptidase (AEP)/LEGUMAIN activated at pH 4.5

Analyse Crystal structure of asparaginyl endopeptidase (AEP)/LEGUMAIN activated at pH… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4NOM
Type
protein
Length
407 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Legumain
EC
3.4.22.34
UniProt
O89017
Pockets
2 · best druggability 0.53

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 14% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ALegumain (EC 3.4.22.34)protein40745% helix, 14% strandO89017

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11030.530.8324empty
2700.450.8217empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 4NOM · Crystal structure of asparaginyl endopeptidase (AEP)/Legumain activated at pH 4.5 · the same entry in another collection · chain A against A, TM-score 1.00
  • O89017 · AlphaFold monomer V2.0 prediction for legumain (O89017) · a predicted model of the same protein · chain A against A, TM-score 0.99

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