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Ligg from sphingobium sp. syk-6 is related to the glutathione transferase omega class

Analyse Ligg from sphingobium sp. syk-6 is related to the glutathione transferase omega… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4G10
Type: protein
Length: 263 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutathione S-transferase homolog
UniProt: Q9WXJ9
Ligands: GSH, SO4
Pockets: 2 · best druggability 0.53

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutathione S-transferase homolog	protein	263	49% helix, 5% strand	Q9WXJ9

Ligands and binding sites

GSH · Glutathione · ligand · chains A
SO4 · Sulfate ion · ion · chains A
ACT · Acetate ion · additive · 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	165	0.53	0.79	29	SO4
2	130	0.47	0.78	23	GSH, ACT

Modifications

Observed in the structure: 8 modified, 1 covalent (engineered, covalent ligand).

Compared structures

4G10 · LigG from Sphingobium sp. SYK-6 is related to the glutathione transferase omega class · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q9WXJ9
Elsewhere: RCSB PDB 4G10 · PDBe 4G10 · UniProt Q9WXJ9

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