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Glutathione transferase from glycine max

Analyse Glutathione transferase from glycine max in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2VO4
Type: protein
Length: 438 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 2,4-D inducible glutathione S-transferase
EC: 2.5.1.18
UniProt: O49235
Ligands: GTB, 4NM
Pockets: 4 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 58% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	2,4-D inducible glutathione S-transferase (EC 2.5.1.18)	protein	219	58% helix, 9% strand	O49235

Ligands and binding sites

GTB · S-(P-nitrobenzyl)glutathione · ligand · 2 copies · chains A, B
4NM · 4-nitrophenyl methanethiol · ligand · 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.

Pockets

4 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	897	0.78	0.80	76	GTB
2	102	0.38	0.75	23	empty
3	68	0.34	0.76	18	empty
4	62	0.31	0.75	17	empty

Interfaces

1 interface between chains.

A–B · 1169 Å² buried · 17 hydrogen bonds · protein-protein

Compared structures

2VO4 · Glutathione transferase from Glycine max · 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
Every structure of UniProt O49235
Elsewhere: RCSB PDB 2VO4 · PDBe 2VO4 · UniProt O49235

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