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Crystal structure of bombyx mori sigma-class glutathione transferase in apo form

Analyse Crystal structure of bombyx mori sigma-class glutathione transferase in apo form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3VPT
Type: protein
Length: 203 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutathione S-transferase sigma
EC: 2.5.1.18
UniProt: Q5CCJ4
Pockets: 1 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 60% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutathione S-transferase sigma (EC 2.5.1.18)	protein	203	60% helix, 8% strand	Q5CCJ4

Ligands and binding sites

PGO · S-1,2-propanediol · additive · 6 copies · chains A
PEG · Di(hydroxyethyl)ether · additive · 4 copies · chains A
PG4 · Tetraethylene glycol · additive · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	133	0.52	0.80	21	PGO

Compared structures

3VPT · Crystal structure of Bombyx mori sigma-class glutathione transferase in apo form · 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 Q5CCJ4
Elsewhere: RCSB PDB 3VPT · PDBe 3VPT · UniProt Q5CCJ4

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