MolNFT v1 · #150053 · protein

Crystal structure of glutathione transferase omega 2S from trametes versicolor

6GIB · Glutathione S-transferase omega-2: “Crystal structure of glutathione transferase omega 2S from trametes versicolor”. X-ray diffraction, 1 ligand (MG), 6 pockets (best druggability 0.78). MolNFT v1 #150053 on GenesisL1: 3D structure…

PDB: 6GIB
Type: protein
Length: 468 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutathione S-transferase omega-2
Ligands: MG
Pockets: 6 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 57% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutathione S-transferase omega-2	protein	231	58% helix, 9% strand	—
B	Glutathione S-transferase omega-2	protein	237	57% helix, 9% strand	—

Ligands and binding sites

MG · Magnesium ion · metal · chains B

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

Pockets

6 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	927	0.78	0.80	91	empty
2	142	0.51	0.79	24	empty
3	169	0.47	0.76	21	empty
4	63	0.43	0.82	18	empty
5	97	0.36	0.75	27	empty

Interfaces

1 interface between chains.

A–B · 958 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

6GIB · Crystal structure of glutathione transferase Omega 2S 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 6GIB · PDBe 6GIB

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