6MHD

Glutathione S-Transferase Omega 1 bound to covalent inhibitor 44

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004364	molecular_function	glutathione transferase activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
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	0014810	biological_process	positive regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion
A	0016491	molecular_function	oxidoreductase activity
A	0016740	molecular_function	transferase activity
A	0019852	biological_process	L-ascorbic acid metabolic process
A	0042178	biological_process	xenobiotic catabolic process
A	0045174	molecular_function	glutathione dehydrogenase (ascorbate) activity
A	0050610	molecular_function	methylarsonate reductase activity
A	0051280	biological_process	negative regulation of release of sequestered calcium ion into cytosol
A	0051281	biological_process	positive regulation of release of sequestered calcium ion into cytosol
A	0070062	cellular_component	extracellular exosome
A	0071243	biological_process	cellular response to arsenic-containing substance
A	0098869	biological_process	cellular oxidant detoxification
B	0004364	molecular_function	glutathione transferase activity
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
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	0014810	biological_process	positive regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion
B	0016491	molecular_function	oxidoreductase activity
B	0016740	molecular_function	transferase activity
B	0019852	biological_process	L-ascorbic acid metabolic process
B	0042178	biological_process	xenobiotic catabolic process
B	0045174	molecular_function	glutathione dehydrogenase (ascorbate) activity
B	0050610	molecular_function	methylarsonate reductase activity
B	0051280	biological_process	negative regulation of release of sequestered calcium ion into cytosol
B	0051281	biological_process	positive regulation of release of sequestered calcium ion into cytosol
B	0070062	cellular_component	extracellular exosome
B	0071243	biological_process	cellular response to arsenic-containing substance
B	0098869	biological_process	cellular oxidant detoxification

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	binding site for residue JRD A 401

Chain	Residue
A	MET29
A	ACN403
A	HOH583
A	CYS32
A	PHE34
A	LEU56
A	VAL72
A	GLY128
A	ILE131
A	ARG132
A	TYR229

---

site_id	AC2
Number of Residues	6
Details	binding site for residue MES A 402

Chain	Residue
A	PHE34
A	GLU85
A	SER86
A	HOH509
A	HOH530
B	GLU118

---

site_id	AC3
Number of Residues	5
Details	binding site for residue ACN A 403

Chain	Residue
A	PRO33
A	VAL127
A	GLY128
A	TRP180
A	JRD401

---

site_id	AC4
Number of Residues	6
Details	binding site for residue MES B 302

Chain	Residue
A	GLU118
B	PHE34
B	LEU71
B	VAL72
B	GLU85
B	SER86

---

site_id	AC5
Number of Residues	5
Details	binding site for residue ACN B 303

Chain	Residue
B	PRO33
B	PRO124
B	VAL127
B	TRP180
B	JRD301

---

site_id	AC6
Number of Residues	14
Details	binding site for Di-peptide JRD B 301 and CYS B 32

Chain	Residue
B	MET29
B	ARG30
B	PHE31
B	PRO33
B	PHE34
B	ALA35
B	GLU36
B	LEU56
B	VAL72
B	GLY128
B	ILE131
B	TYR229
B	ACN303
B	HOH415

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	158
Details	Domain: {"description":"GST N-terminal"}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	248
Details	Domain: {"description":"GST C-terminal"}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"10783391","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10783391","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21106529","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	8
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---