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Crystal structure of glutathione transferase omega 3C from trametes versicolor

Analyse Crystal structure of glutathione transferase omega 3C from trametes versicolor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6SRB
Type: protein
Length: 454 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized protein
Ligands: GSH
Pockets: 4 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 57% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized protein	protein	221	55% helix, 9% strand	—
B	Uncharacterized protein	protein	233	59% helix, 7% strand	—

Ligands and binding sites

GSH · Glutathione · ligand · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	936	0.77	0.79	83	GSH
2	222	0.57	0.79	25	empty
3	114	0.41	0.75	14	empty
4	104	0.36	0.74	18	empty

Interfaces

1 interface between chains.

A–B · 953 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 covalent (covalent ligand).

Compared structures

6SRB · Crystal structure of glutathione transferase Omega 3C from Trametes versicolor · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Elsewhere: RCSB PDB 6SRB · PDBe 6SRB

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