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Crystal structure of recombinant agrocybe aegerita (raal)

Analyse Crystal structure of recombinant agrocybe aegerita (raal) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2ZGL
Type
protein
Length
320 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Anti-tumor lectin
EC
3.1.21.-
UniProt
Q6WY08
Pockets
2 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 3% helix, 52% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BAnti-tumor lectin (EC 3.1.21.-)protein1603% helix, 52% strandQ6WY08

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12120.560.7929empty
2880.430.7923empty

Interfaces

1 interface between chains.

  • A–B · 1030 Ų buried · 9 hydrogen bonds · protein-protein

Compared structures

  • 2ZGL · Crystal structure of recombinant Agrocybe aegerita (rAAL) · the same entry in another collection · chain A against A, TM-score 1.00
  • Q6WY08 · AlphaFold monomer V2.0 prediction for anti-tumor lectin (Q6WY08) · a predicted model of the same protein · chain B against A, TM-score 0.98

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