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Crystal structure of saccharomyces cerevisiae GTT2 in complex with glutathione

Analyse Crystal structure of saccharomyces cerevisiae GTT2 in 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: 3IBH
Type: protein
Length: 208 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Saccharomyces cerevisiae GTT2
EC: 2.5.1.18
UniProt: Q12390
Ligands: GSH
Pockets: 2 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 59% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Saccharomyces cerevisiae GTT2 (EC 2.5.1.18)	protein	208	59% helix, 8% strand	Q12390

Ligands and binding sites

GSH · Glutathione · ligand · chains A

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

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	310	0.63	0.79	35	GSH
2	62	0.36	0.78	16	empty

Compared structures

3IBH · Crystal structure of Saccharomyces cerevisiae Gtt2 in complex with glutathione · the same entry in another collection · chain A against A, TM-score 1.00
Q12390 · AlphaFold monomer V2.0 prediction for glutathione S-transferase 2 (Q12390) · a predicted model of the same protein · chain A against A, TM-score 0.99

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q12390
Elsewhere: RCSB PDB 3IBH · PDBe 3IBH · UniProt Q12390

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