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Crystal structure of poplar glutathione transferase U20 in complex with baicalein

Analyse Crystal structure of poplar glutathione transferase U20 in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 8A0Q
Type: protein
Length: 215 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutathione transferase
EC: 2.5.1.18
UniProt: D2X9R3
Ligands: 3WL, CL
Pockets: 4 · best druggability 0.55

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutathione transferase (EC 2.5.1.18)	protein	215	58% helix, 9% strand	D2X9R3

Ligands and binding sites

3WL · 5,6,7-trihydroxy-2-phenyl-4H-chromen-4-one · ligand · chains A
CL · Chloride ion · ion · chains A

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	225	0.55	0.77	22	3WL
2	59	0.36	0.78	11	empty
3	66	0.32	0.75	19	empty
4	55	0.30	0.76	13	CL

Compared structures

8A0Q · Crystal structure of poplar glutathione transferase U20 in complex with baicalein · 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 D2X9R3
Elsewhere: RCSB PDB 8A0Q · PDBe 8A0Q · UniProt D2X9R3

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