4gtu Summary

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

The structure was published by Patskovsky, Y.V., Patskovska, L.N., and Listowsky, I., in 1999 in a paper entitled "An asparagine-phenylalanine substitution accounts for catalytic differences between hGSTM3-3 and other human class mu glutathione S-transferases." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 3.3 Å and deposited in 1999.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of GLUTATHIONE S-TRANSFERASE.

The molecule has more than one probable quaternary state observed. For more details see the quaternary structure page.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A GLUTATHIONE S-TRANSFERASE Q03013 (2-218) (GSTM4_HUMAN)search Homo sapienssearch 100% 217 100%
B GLUTATHIONE S-TRANSFERASE Q03013 (2-218) (GSTM4_HUMAN)search Homo sapienssearch 100% 217 100%
C GLUTATHIONE S-TRANSFERASE Q03013 (2-218) (GSTM4_HUMAN)search Homo sapienssearch 100% 217 100%
D GLUTATHIONE S-TRANSFERASE Q03013 (2-218) (GSTM4_HUMAN)search Homo sapienssearch 100% 217 100%
E GLUTATHIONE S-TRANSFERASE Q03013 (2-218) (GSTM4_HUMAN)search Homo sapienssearch 100% 217 100%
F GLUTATHIONE S-TRANSFERASE Q03013 (2-218) (GSTM4_HUMAN)search Homo sapienssearch 100% 217 100%
G GLUTATHIONE S-TRANSFERASE Q03013 (2-218) (GSTM4_HUMAN)search Homo sapienssearch 100% 217 100%
H GLUTATHIONE S-TRANSFERASE Q03013 (2-218) (GSTM4_HUMAN)search Homo sapienssearch 100% 217 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q03013 (2 - 218) GLUTATHIONE S-TRANSFERASE Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B, C, D, E, F, G, H (Q03013) Glutathione S-transferase (GST), C-terminal domainsearch, Glutathione S-transferase (GST), N-terminal domainsearch Glutaredoxinsearch, Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2search PF00043: Glutathione S-transferase, C-terminal domainsearch, PF02798: Glutathione S-transferase, N-terminal domainsearch

Chain ID Cellular component (GO) Biological process (GO) Molecular function (GO)
A, B, C, D, E, F, G, H (Q03013) cytoplasmsearch cytosolsearch glutathione metabolic processsearch glutathione derivative biosynthetic processsearch xenobiotic metabolic processsearch small molecule metabolic processsearch xenobiotic catabolic processsearch metabolic processsearch enzyme bindingsearch glutathione transferase activitysearch protein homodimerization activitysearch glutathione bindingsearch transferase activitysearch

Chain InterPro annotation
A, B, C, D, E, F, G, H Glutathione S-transferase, Mu classsearch Glutathione S-transferase, N-terminalsearch Glutathione S-transferase, C-terminalsearch Glutathione S-transferase, C-terminal-likesearch Thioredoxin-like foldsearch