2GTU

LIGAND-FREE HUMAN GLUTATHIONE S-TRANSFERASE M2-2 (E.C.2.5.1.18), MONOCLINIC CRYSTAL FORM

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004364	molecular_function	glutathione transferase activity
A	0004602	molecular_function	glutathione peroxidase activity
A	0005504	molecular_function	fatty acid binding
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006629	biological_process	lipid metabolic process
A	0006749	biological_process	glutathione metabolic process
A	0010880	biological_process	regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
A	0010881	biological_process	regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
A	0014809	biological_process	regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion
A	0016529	cellular_component	sarcoplasmic reticulum
A	0016740	molecular_function	transferase activity
A	0018916	biological_process	nitrobenzene metabolic process
A	0019855	molecular_function	calcium channel inhibitor activity
A	0019899	molecular_function	enzyme binding
A	0042178	biological_process	xenobiotic catabolic process
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0043295	molecular_function	glutathione binding
A	0043651	biological_process	linoleic acid metabolic process
A	0044325	molecular_function	transmembrane transporter binding
A	0051122	biological_process	hepoxilin biosynthetic process
A	0055119	biological_process	relaxation of cardiac muscle
A	0070062	cellular_component	extracellular exosome
A	0070458	biological_process	cellular detoxification of nitrogen compound
A	0071313	biological_process	cellular response to caffeine
A	0098869	biological_process	cellular oxidant detoxification
B	0004364	molecular_function	glutathione transferase activity
B	0004602	molecular_function	glutathione peroxidase activity
B	0005504	molecular_function	fatty acid binding
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006629	biological_process	lipid metabolic process
B	0006749	biological_process	glutathione metabolic process
B	0010880	biological_process	regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
B	0010881	biological_process	regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
B	0014809	biological_process	regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion
B	0016529	cellular_component	sarcoplasmic reticulum
B	0016740	molecular_function	transferase activity
B	0018916	biological_process	nitrobenzene metabolic process
B	0019855	molecular_function	calcium channel inhibitor activity
B	0019899	molecular_function	enzyme binding
B	0042178	biological_process	xenobiotic catabolic process
B	0042802	molecular_function	identical protein binding
B	0042803	molecular_function	protein homodimerization activity
B	0043295	molecular_function	glutathione binding
B	0043651	biological_process	linoleic acid metabolic process
B	0044325	molecular_function	transmembrane transporter binding
B	0051122	biological_process	hepoxilin biosynthetic process
B	0055119	biological_process	relaxation of cardiac muscle
B	0070062	cellular_component	extracellular exosome
B	0070458	biological_process	cellular detoxification of nitrogen compound
B	0071313	biological_process	cellular response to caffeine
B	0098869	biological_process	cellular oxidant detoxification

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	172
Details	Domain: {"description":"GST N-terminal"}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	236
Details	Domain: {"description":"GST C-terminal"}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16549767","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19808963","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P08010","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	2
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI6
Number of Residues	2
Details	Site: {"description":"Important for substrate specificity"}

Chain

Residue

Details

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site_id	SWS_FT_FI7
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P08010","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1oe8

Chain	Residue	Details
A	TYR6

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site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1oe8

Chain	Residue	Details
B	TYR6

---