Structure of PDB 6ssu Chain A

Receptor sequence

>6ssuA (length=139) Species: 9606 (Homo sapiens) [Search protein sequence]

NSILLAAVSILSACQQSYFALQVGKARLKYKVTPPAVTGSPEFERVFRAQ
QNCVEFYPIFIITLWMAGWYFNQVFATCLGLVYIYGRHLYFWGYSEAAKK
RITGFRLSLGILALLTLLGALGIANSFLDEYLDLNIAKK

3D structure

PDB

6ssu Crystal structures of human MGST2 reveal synchronized conformational changes regulating catalysis.

Chain

Resolution

2.499 Å

3D
structure

Enzymatic activity

Enzyme Commision number

1.11.1.-
2.5.1.18: glutathione transferase.
4.4.1.20: leukotriene-C4 synthase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	GSH	A	R51 N55 Y93 Y97 R104 F108	R48 N52 Y90 Y94 R101 F105
BS02	GSH	A	A23 V26 R30 Q53	A20 V23 R27 Q50

Gene Ontology

	Molecular Function
GO:0004364	glutathione transferase activity
GO:0004464	leukotriene-C4 synthase activity
GO:0004602	glutathione peroxidase activity
GO:0005515	protein binding
GO:0008047	enzyme activator activity
GO:0016491	oxidoreductase activity
GO:0016740	transferase activity
GO:0016829	lyase activity
GO:0042802	identical protein binding
GO:0043295	glutathione binding

	Biological Process
GO:0006629	lipid metabolic process
GO:0006691	leukotriene metabolic process
GO:0006750	glutathione biosynthetic process
GO:0019370	leukotriene biosynthetic process
GO:0032496	response to lipopolysaccharide
GO:0046466	membrane lipid catabolic process
GO:0050729	positive regulation of inflammatory response
GO:0098869	cellular oxidant detoxification

	Cellular Component
GO:0005635	nuclear envelope
GO:0005783	endoplasmic reticulum
GO:0005789	endoplasmic reticulum membrane
GO:0005886	plasma membrane
GO:0016020	membrane
GO:0043231	intracellular membrane-bounded organelle

External links

PDB	RCSB:6ssu, PDBe:6ssu, PDBj:6ssu
PDBsum	6ssu
PubMed	33741927
UniProt	Q99735\|MGST2_HUMAN Microsomal glutathione S-transferase 2 (Gene Name=MGST2)