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The structure of DHAR1 from arabidopsis thaliana

Analyse The structure of DHAR1 from arabidopsis thaliana in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5ELG
Type: protein
Length: 212 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutathione S-transferase DHAR1, mitochondrial
EC: 2.5.1.18
UniProt: Q9FWR4
Ligands: GSH
Pockets: 2 · best druggability 0.40

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutathione S-transferase DHAR1, mitochondrial (EC 2.5.1.18)	protein	212	50% helix, 14% strand	Q9FWR4

Ligands and binding sites

GSH · Glutathione · ligand · chains A
GOL · Glycerol · additive · 5 copies · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	78	0.40	0.79	26	empty
2	92	0.35	0.74	15	GOL, GSH

Compared structures

5ELG · The structure of DHAR1 from Arabidopsis thaliana · the same entry in another collection · chain A against A, TM-score 1.00
Q9FWR4 · AlphaFold monomer V2.0 prediction for glutathione S-transferase DHAR1, mitochondrial… · 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 Q9FWR4
Elsewhere: RCSB PDB 5ELG · PDBe 5ELG · UniProt Q9FWR4

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