Structure of PDB 3ktl Chain B

Receptor sequence

>3ktlB (length=219) Species: 9606 (Homo sapiens)

KPKLHYFNARGRMESTRWLLAAAGVEFEEKFIKSAEDLDKLRNDGYLMFQ
QVPMVEIDGMKLVQTRAALNYIASKYNLYGKDIKERALIDMYIEGIADLG
EMILLLPVCPPEEKDAKLALIKEKIKNRYFPAFEKVLKSHGQDYLVGNKL
SRADIHLVELLYYVEELDSSLISSFPLLKALKTRISNLPTVKKFLQPGSP
RKPPMDEKSLEEARKIFRF

3D structure

• PDB: 3ktl The role of a topologically conserved isoleucine in glutathione transferase structure, stability and function.
• Chain: B
• Resolution: 1.75 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Y9 R15 R20
• Catalytic site (residue number reindexed from 1): Y6 R12 R17
• Enzyme Commision number: 1.11.1.-
  2.5.1.18: glutathione transferase.
  5.3.3.-

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	GTX	B	D101 R131	D98 R128
BS02	GTX	B	R15 R45 Q54 V55 Q67 T68 M208 F220	R12 R42 Q51 V52 Q64 T65 M205 F217

Gene Ontology

Molecular Function

• GO:0004364 glutathione transferase activity
• GO:0004601 peroxidase activity
• GO:0004602 glutathione peroxidase activity
• GO:0004769 steroid delta-isomerase activity
• GO:0005504 fatty acid binding
• GO:0005515 protein binding
• GO:0016740 transferase activity
• GO:0016853 isomerase activity

Biological Process

• GO:0006629 lipid metabolic process
• GO:0006693 prostaglandin metabolic process
• GO:0006749 glutathione metabolic process
• GO:0006805 xenobiotic metabolic process
• GO:0030855 epithelial cell differentiation
• GO:0043651 linoleic acid metabolic process
• GO:0098869 cellular oxidant detoxification
• GO:1901687 glutathione derivative biosynthetic process

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol
• GO:0070062 extracellular exosome

External links

• PDB: RCSB:3ktl, PDBe:3ktl, PDBj:3ktl
• PDBsum: 3ktl
• PubMed: 20606271
• UniProt: P08263|GSTA1_HUMAN Glutathione S-transferase A1 (Gene Name=GSTA1)