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LIGAND-FREE HOMODIMERIC HUMAN GLUTATHIONE S-TRANSFERASE M4-4

Source organism: Homo sapiens
Biochemical function: glutathione binding
Biological process: long-chain fatty acid biosynthetic process
Cellular component: intercellular bridge

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EC 4.4.1.20: Leukotriene-C(4) synthase

Reaction catalysed:
Leukotriene C(4) = leukotriene A(4) + glutathione
Systematic name:
Leukotriene-C(4) glutathione-lyase (leukotriene-A(4)-forming)
Alternative Name(s):
  • (7E,9E,11Z,14Z)-(5S,6R)-5,6-epoxyicosa-7,9,11,14-tetraenoate:glutathione leukotriene-transferase (epoxide-ring-opening)
  • (7E,9E,11Z,14Z)-(5S,6R)-6-(glutathion-S-yl)-5-hydroxyicosa-7,9,11,14-tetraenoate glutathione-lyase (epoxide-forming)
  • LTC(4) synthase
  • LTC(4) synthetase
  • Leukotriene A(4):glutathione S-leukotrienyltransferase
  • Leukotriene C(4) synthetase

EC 2.5.1.18: Glutathione transferase

Reaction catalysed:
RX + glutathione = HX + R-S-glutathione
Systematic name:
RX:glutathione R-transferase
Alternative Name(s):
  • Glutathione S-alkyl transferase
  • Glutathione S-alkyltransferase
  • Glutathione S-aralkyltransferase
  • Glutathione S-aryltransferase
  • Glutathione S-transferase
  • S-(hydroxyalkyl)glutathione lyase

GO terms

Sequence families

Pfam Protein families (Pfam)
PF00043
Domain description: Glutathione S-transferase, C-terminal domain
Occurring in:
  1. Glutathione S-transferase Mu 4

PF02798
Domain description: Glutathione S-transferase, N-terminal domain
Occurring in:
  1. Glutathione S-transferase Mu 4
The deposited structure of PDB entry 4gtu contains 8 copies of Pfam domain PF02798 (Glutathione S-transferase, N-terminal domain) in Glutathione S-transferase Mu 4. Showing 1 copy in chain A.

InterPro InterPro annotations
IPR003081
Domain description: Glutathione S-transferase, Mu class
Occurring in:
  1. Glutathione S-transferase Mu 4
IPR004045
Domain description: Glutathione S-transferase, N-terminal
Occurring in:
  1. Glutathione S-transferase Mu 4
IPR004046
Domain description: Glutathione S-transferase, C-terminal
Occurring in:
  1. Glutathione S-transferase Mu 4
IPR010987
Domain description: Glutathione S-transferase, C-terminal-like
Occurring in:
  1. Glutathione S-transferase Mu 4
IPR036282
Domain description: Glutathione S-transferase, C-terminal domain superfamily
Occurring in:
  1. Glutathione S-transferase Mu 4
IPR036249
Domain description: Thioredoxin-like superfamily
Occurring in:
  1. Glutathione S-transferase Mu 4
IPR040079
Domain description: Glutathione transferase family
Occurring in:
  1. Glutathione S-transferase Mu 4

Structure domains

CATH CATH domains
3.40.30.10
Class: Alpha Beta
Architecture: 3-Layer(aba) Sandwich
Topology: Glutaredoxin
Homology: Glutaredoxin
Occurring in:
  1. Glutathione S-transferase Mu 4
The deposited structure of PDB entry 4gtu contains 8 copies of CATH domain 3.40.30.10 (Glutaredoxin) in Glutathione S-transferase Mu 4. Showing 1 copy in chain A.
1.20.1050.10
Class: Mainly Alpha
Architecture: Up-down Bundle
Topology: Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2
Homology: Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2
Occurring in:
  1. Glutathione S-transferase Mu 4
The deposited structure of PDB entry 4gtu contains 8 copies of CATH domain 1.20.1050.10 (Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2) in Glutathione S-transferase Mu 4. Showing 1 copy in chain A.
SCOP SCOP annotations
47617
Class: All alpha proteins
Fold: GST C-terminal domain-like
Superfamily: GST C-terminal domain-like
Occurring in:
  1. Glutathione S-transferase Mu 4
The deposited structure of PDB entry 4gtu contains 8 copies of SCOP domain 47617 (Glutathione S-transferase (GST), C-terminal domain) in Glutathione S-transferase Mu 4. Showing 1 copy in chain A.
52862
Class: Alpha and beta proteins (a/b)
Fold: Thioredoxin fold
Superfamily: Thioredoxin-like
Occurring in:
  1. Glutathione S-transferase Mu 4
The deposited structure of PDB entry 4gtu contains 8 copies of SCOP domain 52862 (Glutathione S-transferase (GST), N-terminal domain) in Glutathione S-transferase Mu 4. Showing 1 copy in chain A.

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