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Structure of the thaumatin-like xylanase inhibitor tlxi

Analyse Structure of the thaumatin-like xylanase inhibitor tlxi in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3G7M
Type
protein
Length
151 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Xylanase inhibitor tl-XI
UniProt
Q0WX48
Ligands
NA
Pockets
1 · best druggability 0.26

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 42% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AXylanase inhibitor tl-XIprotein1510% helix, 42% strandQ0WX48

Ligands and binding sites

  • NA · Sodium ion · metal · chains A
  • GOL · Glycerol · additive · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1500.260.7417empty

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

  • 3G7M · Structure of the thaumatin-like xylanase inhibitor TLXI · the same entry in another collection · chain A against A, TM-score 1.00

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