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Crystal structure analysis of colorado potato beetle glutathione-S transferase LDGSTU1

Analyse Crystal structure analysis of colorado potato beetle 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: 7RKA
Type: protein
Length: 422 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutathione S-transferase U1
EC: 2.5.1.18
UniProt: A0A1P8PEY0
Ligands: GSH
Pockets: 4 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 61% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Glutathione S-transferase U1 (EC 2.5.1.18)	protein	211	61% helix, 9% strand	A0A1P8PEY0

Ligands and binding sites

GSH · Glutathione · ligand · 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	228	0.55	0.78	23	empty
2	214	0.49	0.75	29	GSH
3	75	0.41	0.79	17	empty
4	104	0.38	0.75	21	empty

Interfaces

1 interface between chains.

A–B · 295 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

7RKA · Crystal structure analysis of Colorado potato beetle glutathione-S transferase LdGSTu1 · 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 A0A1P8PEY0
Elsewhere: RCSB PDB 7RKA · PDBe 7RKA · UniProt A0A1P8PEY0

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