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Crystal structure of glutathione S transferase in complex with glutathione from pseudomonas fluorescens

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

PDB: 3M0F
Type: protein
Length: 405 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized protein GST_N
UniProt: Q4KDJ6
Ligands: GSH
Pockets: 3 · best druggability 0.86

Structure

x-ray diffraction · 2 distinct chains · 61% helix, 6% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized protein GST_N	protein	203	61% helix, 6% strand	Q4KDJ6
B	Uncharacterized protein GST_N	protein	202	61% helix, 6% strand	Q4KDJ6

Ligands and binding sites

GSH · Glutathione · ligand · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	834	0.86	0.88	82	GSH
2	308	0.69	0.84	38	empty
3	82	0.39	0.78	20	empty

Interfaces

1 interface between chains.

A–B · 2175 Å² buried · 38 hydrogen bonds · protein-protein

Compared structures

3M0F · Crystal structure of Glutathione S Transferase in complex with glutathione from… · 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 Q4KDJ6
Elsewhere: RCSB PDB 3M0F · PDBe 3M0F · UniProt Q4KDJ6

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