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Crystal structure of poplar glutathione transferase U20 in complex with pinocembrin

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: 8A0R
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: KML, CL
Pockets: 3 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 60% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutathione transferase (EC 2.5.1.18)	protein	215	60% helix, 9% strand	D2X9R3

Ligands and binding sites

KML · pinocembrin · ligand · chains A
CL · Chloride ion · ion · chains A
TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A

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

Pockets

3 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	219	0.56	0.78	24	KML
2	78	0.38	0.77	12	empty
3	56	0.30	0.75	13	empty

Compared structures

8A0R · Crystal structure of poplar glutathione transferase U20 in complex with pinocembrin · 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 8A0R · PDBe 8A0R · UniProt D2X9R3

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