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Structure of wuchereria bancrofti pi-class glutathione S-transferase

Analyse Structure of wuchereria bancrofti pi-class glutathione S-transferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5D73
Type: protein
Length: 414 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutathione S-transferase
UniProt: Q86LL8
Ligands: GSH
Pockets: 5 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 60% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Glutathione S-transferase	protein	207	60% helix, 10% strand	Q86LL8

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

5 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	773	0.74	0.79	70	GSH
2	66	0.37	0.79	18	empty
3	74	0.37	0.77	15	empty
4	72	0.36	0.77	15	empty
5	50	0.27	0.75	14	empty

Interfaces

1 interface between chains.

A–B · 1416 Å² buried · 28 hydrogen bonds · protein-protein

Compared structures

5D73 · Structure of Wuchereria bancrofti pi-class glutathione S-transferase · 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 Q86LL8
Elsewhere: RCSB PDB 5D73 · PDBe 5D73 · UniProt Q86LL8

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