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Arabidopsis thaliana GSTF9, GSO3 and gsoh bound

Analyse Arabidopsis thaliana GSTF9, GSO3 and gsoh bound in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6F01
Type: protein
Length: 417 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: O80852
Ligands: GTS, GS8, BR

Structure

x-ray diffraction · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	205	—	O80852
B	—	protein	212	—	O80852

Ligands and binding sites

GTS · Glutathione sulfonic acid · ligand · chains A, B
GS8 · S-Hydroxy-Glutathione · ligand · chains B
BR · Bromide ion · ion · 2 copies · chains A, B
GOL · Glycerol · additive · 2 copies · chains A, B

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

Compared structures

6F01 · Arabidopsis thaliana GSTF9, GSO3 and gsoh bound · the same entry in another collection · chain A against A, TM-score 1.00
O80852 · AlphaFold monomer V2.0 prediction for glutathione S-transferase F9 (O80852) · 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 O80852
Elsewhere: RCSB PDB 6F01 · PDBe 6F01 · UniProt O80852

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