GL1X · GenesisL1 explorer

Research workbench

Crystal structure of the helical domain of S. pombe TAZ1

Analyse Crystal structure of the helical domain of S. pombe TAZ1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4ZMI
Type
protein
Length
235 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Telomere length regulator TAZ1
UniProt
P79005
Ligands
MG, CO
Pockets
1 · best druggability 0.33

Structure

x-ray diffraction · 1 distinct chain · 69% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATelomere length regulator TAZ1protein23569% helix, 0% strandP79005

Ligands and binding sites

  • MG · Magnesium ion · metal · chains A
  • CO · Cobalt (II) ion · metal · 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
1580.330.7711empty

Compared structures

  • 4ZMI · Crystal structure of the Helical domain of S. pombe Taz1 · the same entry in another collection · chain A against A, TM-score 1.00
  • P79005 · AlphaFold monomer V2.0 prediction for telomere length regulator TAZ1 (P79005) · a predicted model of the same protein · chain A against A, TM-score 1.00

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.