Uniprot accession / id : P48774  OR   Uniprot accession / id : P21266  OR   Uniprot accession / id : Q6FGJ9
 
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Entry Information
Entry status  (1)
REL
(1)
 
Experimental methods  (1)
X-ray diffraction
(1)
 
Authors  (3)
Listowsky I
(1)
Patskovska LN
(1)
Patskovsky YV
(1)
 
Homo / hetero assembly  (1)
hetero
(1)
 
Assembly composition  (1)
protein/protein complex
(1)
 
Assembly polymer count  (1)
dimer
(1)
 
Resolution distribution
2.5 - 3
(1)
 
Release year distribution
1995 - 2000
(1)
 
Journal  (1)
Biochemistry
(1)
 
Macromolecules
Organism superkingdom  (1)
Eukaryota
(1)
 
Organism name  (1)
Homo sapiens
(1)
 
Molecule name  (4)
GST class-mu 3
(1)
GSTM3-3
(1)
Glutathione S-transferase Mu 3
(1)
hGSTM3-3
(1)
 
Molecule type  (1)
Protein
(1)
 
Gene names  (2)
GST5
(1)
GSTM3
(1)
 
Interacting Molecules  (1)
Glutathione S-transferase Mu 2
(1)
 
Function and Biology
EC number / name  (1)
2.5.1.18 : Glutathione transferase
(1)
 
Biological function  (7)
enzyme binding
(1)
glutathione binding
(1)
glutathione transferase activity
(1)
identical protein binding
(1)
protein binding
(1)
protein homodimerization activity
(1)
transferase activity
(1)
 
Biological process  (6)
cellular detoxification of nitrogen compound
(1)
establishment of blood-nerve barrier
(1)
glutathione metabolic process
(1)
nitrobenzene metabolic process
(1)
response to estrogen
(1)
xenobiotic catabolic process
(1)
 
Biological cell component  (6)
cytoplasm
(1)
cytosol
(1)
extracellular exosome
(1)
intercellular bridge
(1)
nucleus
(1)
sperm fibrous sheath
(1)
 
Sequence and Structure classification
SCOP fold  (2)
GST C-terminal domain-like
(1)
Thioredoxin fold
(1)
 
SCOP family  (2)
Glutathione S-transferase (GST), C-terminal domain
(1)
Glutathione S-transferase (GST), N-terminal domain
(1)
 
CATH class  (2)
Alpha Beta
(1)
Mainly Alpha
(1)
 
CATH topology  (2)
Glutaredoxin
(1)
Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2
(1)
 
Pfam accession / name  (2)
PF00043 : GST_C
(1)
PF02798 : GST_N
(1)
 
Experimental Information
Diffraction radiation source type  (1)
Rotating anode
(1)
 
Diffraction source  (1)
RIGAKU RUH2R
(1)
 
Diffraction detector type  (1)
Area detector
(1)
 
Refinement software  (1)
X-PLOR
(1)
 
Representative Structures
Representative Structures
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LIGAND-FREE HETERODIMERIC HUMAN GLUTATHIONE S-TRANSFERASE M2-3 (EC 2.5.1.18), MONOCLINIC CRYSTAL FORM
Patskovsky YV, Patskovska LN, Listowsky I
Biochemistry (1999) [PMID: 10587441  ]
Source organism: Homo sapiens  
Assembly composition: protein/protein complex
Assembly name: Glutathione S-transferase Mu 2 and Glutathione S-transferase Mu 3 (Preferred)   search this complex
PDBe complex ID: PDB-CPX-149195 (Preferred)   search this ID
PDBe-KB: P21266    P28161   
X-ray diffraction
2.8Å resolution
Released: 29 Jul 1999
Model geometry
Fit model/data
3gtu
3gtu
3gtu
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