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Transglutaminase from geobacillus stearothermophilus (without C- terminal extension)

Analyse Transglutaminase from geobacillus stearothermophilus (without C- terminal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7C9J
Type
protein
Length
207 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein-glutamine gamma-glutamyltransferase
EC
2.3.2.13
UniProt
A0A3L7D5Y5
Pockets
1 · best druggability 0.36

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein-glutamine gamma-glutamyltransferase (EC 2.3.2.13)protein20739% helix, 23% strandA0A3L7D5Y5

Ligands and binding sites

  • EDO · 1,2-ethanediol · additive · 5 copies · chains A
  • CIT · Citric acid · 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
1960.360.7524empty

Modifications

Observed in the structure: 1 modified (oxidation).

Compared structures

  • 7C9J · Transglutaminase from Geobacillus stearothermophilus (without C-terminal extension) · the same entry in another collection · chain A against A, TM-score 1.00

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