Research workbench

Crystal structure of aedes aegypti noppera-bo, glutathione S- transferase epsilon 8, in desmethylglycitein and glutathione-bound form

Analyse Crystal structure of aedes aegypti noppera-bo, 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: 7EBW
Type: protein
Length: 875 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutathione transferase
UniProt: A0A1S4FIB3
Ligands: GSH, 674, CA
Pockets: 8 · best druggability 0.71

Structure

x-ray diffraction · 4 distinct chains · 58% helix, 7% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutathione transferase	protein	219	57% helix, 7% strand	A0A1S4FIB3
B	Glutathione transferase	protein	221	56% helix, 7% strand	A0A1S4FIB3
C	Glutathione transferase	protein	216	59% helix, 7% strand	A0A1S4FIB3
D	Glutathione transferase	protein	219	59% helix, 7% strand	A0A1S4FIB3

Ligands and binding sites

GSH · Glutathione · ligand · 4 copies · chains A, B, C, D
674 · 6,7-dihydroxy-3-(4-hydroxyphenyl)-4H-chromen-4-one · ligand · 4 copies · chains A, B, C, D
CA · Calcium ion · metal · 8 copies · chains A, D, B, C

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

Pockets

8 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	307	0.71	0.84	53	empty
2	385	0.70	0.82	39	GSH, 674
3	316	0.64	0.80	27	GSH, 674
4	307	0.63	0.80	28	GSH, 674
5	166	0.63	0.85	34	empty

Interfaces

6 interfaces between chains.

B–C · 493 Å² buried · 5 hydrogen bonds · protein-protein
A–B · 415 Å² buried · 14 hydrogen bonds · protein-protein
B–D · 380 Å² buried · 3 hydrogen bonds · protein-protein
A–D · 359 Å² buried · 6 hydrogen bonds · protein-protein
A–C · 234 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

7EBW · Crystal structure of Aedes aegypti Noppera-bo, glutathione S-transferase epsilon 8, in… · 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 A0A1S4FIB3
Elsewhere: RCSB PDB 7EBW · PDBe 7EBW · UniProt A0A1S4FIB3

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.