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Solution structure of human thioltransferase complex with glutathione

Analyse Solution structure of human thioltransferase complex with glutathione in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1B4Q
Type
protein
Length
105 residues
Chains
1
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein (human thioltransferase)
UniProt
P35754
Ligands
GSH

Structure

solution nmr · 1 distinct chain · 47% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein (human thioltransferase)protein10547% helix, 19% strandP35754

Ligands and binding sites

  • GSH · Glutathione · ligand · chains A

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

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

  • 1B4Q · Solution structure of human thioltransferase complex with glutathione · the same entry in another collection · chain A against A, TM-score 1.00
  • P35754 · AlphaFold monomer V2.0 prediction for glutaredoxin-1 (P35754) · a predicted model of the same protein · chain A against A, TM-score 0.95

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