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3D structure of TET3 from pyrococcus horikoshii

Analyse 3D structure of TET3 from pyrococcus horikoshii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2WZN
Type
protein
Length
338 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
354AA long hypothetical operon protein frv
UniProt
O59485
Ligands
ZN, CL
Pockets
1 · best druggability 0.42

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A354AA long hypothetical operon protein frvprotein33830% helix, 27% strandO59485

Ligands and binding sites

  • ZN · Zinc ion · metal · 2 copies · chains A
  • CL · Chloride ion · ion · 2 copies · chains A
  • GOL · Glycerol · additive · 2 copies · 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
11090.420.7822CL

Compared structures

  • 2WZN · 3d structure of TET3 from Pyrococcus horikoshii · the same entry in another collection · chain A against A, TM-score 1.00

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