Structure of PDB 1xwk Chain B

Receptor sequence

>1xwkB (length=217) Species: 9606 (Homo sapiens)

PMILGYWDIRGLAHAIRLLLEYTDSSYEEKKYTMGDAPDYDRSQWLNEKF
KLGLDFPNLPYLIDGAHKITQSNAILCYIARKHNLCGETEEEKIRVDILE
NQTMDNHMQLGMICYNPEFEKLKPKYLEELPEKLKLYSEFLGKRPWFAGN
KITFVDFLVYDVLDLHRIFEPKCLDAFPNLKDFISRFEGLEKISAYMKSS
RFLPRPVFSKMAVWGNK

3D structure

• PDB: 1xwk Transition state model and mechanism of nucleophilic aromatic substitution reactions catalyzed by human glutathione S-transferase M1a-1a.
• Chain: B
• Resolution: 2.3 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Y6 L12
• Catalytic site (residue number reindexed from 1): Y6 L12
• Enzyme Commision number: 2.5.1.18: glutathione transferase.

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	GDN	B	L12 R42 W45 K49 N58 L59 Q71 S72 H107 M108	L12 R42 W45 K49 N58 L59 Q71 S72 H107 M108

Gene Ontology

Molecular Function

• GO:0004364 glutathione transferase activity
• GO:0016740 transferase activity
• GO:0019899 enzyme binding
• GO:0042802 identical protein binding
• GO:0042803 protein homodimerization activity
• GO:0043295 glutathione binding

Biological Process

• GO:0006629 lipid metabolic process
• GO:0006693 prostaglandin metabolic process
• GO:0006749 glutathione metabolic process
• GO:0018916 nitrobenzene metabolic process
• GO:0042178 xenobiotic catabolic process
• GO:0051122 hepoxilin biosynthetic process
• GO:0070458 cellular detoxification of nitrogen compound
• GO:1901687 glutathione derivative biosynthetic process

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol
• GO:0045171 intercellular bridge

External links

• PDB: RCSB:1xwk, PDBe:1xwk, PDBj:1xwk
• PDBsum: 1xwk
• PubMed: 16548513
• UniProt: P09488|GSTM1_HUMAN Glutathione S-transferase Mu 1 (Gene Name=GSTM1)