1YJ6

crystal structure of human glutathione S-transferase M1A-1A complexed with glutathionyl-zinc-trihydroxide

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004364	molecular_function	glutathione transferase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006629	biological_process	lipid metabolic process
A	0006693	biological_process	prostaglandin metabolic process
A	0006749	biological_process	glutathione metabolic process
A	0016740	molecular_function	transferase activity
A	0018916	biological_process	nitrobenzene metabolic process
A	0019899	molecular_function	enzyme binding
A	0042178	biological_process	xenobiotic catabolic process
A	0042803	molecular_function	protein homodimerization activity
A	0043295	molecular_function	glutathione binding
A	0051122	biological_process	hepoxilin biosynthetic process
A	0070458	biological_process	cellular detoxification of nitrogen compound
A	1901687	biological_process	glutathione derivative biosynthetic process
B	0004364	molecular_function	glutathione transferase activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006629	biological_process	lipid metabolic process
B	0006693	biological_process	prostaglandin metabolic process
B	0006749	biological_process	glutathione metabolic process
B	0016740	molecular_function	transferase activity
B	0018916	biological_process	nitrobenzene metabolic process
B	0019899	molecular_function	enzyme binding
B	0042178	biological_process	xenobiotic catabolic process
B	0042803	molecular_function	protein homodimerization activity
B	0043295	molecular_function	glutathione binding
B	0051122	biological_process	hepoxilin biosynthetic process
B	0070458	biological_process	cellular detoxification of nitrogen compound
B	1901687	biological_process	glutathione derivative biosynthetic process
C	0004364	molecular_function	glutathione transferase activity
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006629	biological_process	lipid metabolic process
C	0006693	biological_process	prostaglandin metabolic process
C	0006749	biological_process	glutathione metabolic process
C	0016740	molecular_function	transferase activity
C	0018916	biological_process	nitrobenzene metabolic process
C	0019899	molecular_function	enzyme binding
C	0042178	biological_process	xenobiotic catabolic process
C	0042803	molecular_function	protein homodimerization activity
C	0043295	molecular_function	glutathione binding
C	0051122	biological_process	hepoxilin biosynthetic process
C	0070458	biological_process	cellular detoxification of nitrogen compound
C	1901687	biological_process	glutathione derivative biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 219

Chain	Residue
A	GSH218
A	HOH257
A	HOH258
A	HOH259

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 219

Chain	Residue
B	GSH218
B	HOH251
B	HOH252
B	HOH253

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 219

Chain	Residue
C	HOH249
C	HOH250
C	HOH251
C	GSH218

---

site_id	AC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE GSH A 218

Chain	Residue
A	TRP7
A	LEU12
A	ARG42
A	TRP45
A	LYS49
A	ASN58
A	LEU59
A	GLN71
A	SER72
A	ZN219
A	HOH228
B	ASP105

---

site_id	AC5
Number of Residues	15
Details	BINDING SITE FOR RESIDUE GSH B 218

Chain	Residue
A	ASP105
B	TRP7
B	LEU12
B	ARG42
B	TRP45
B	LYS49
B	ASN58
B	LEU59
B	GLN71
B	SER72
B	MET104
B	ZN219
B	HOH232
B	HOH243
B	HOH253

---

site_id	AC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE GSH C 218

Chain	Residue
C	TYR6
C	LEU12
C	TRP45
C	LYS49
C	ASN58
C	LEU59
C	GLN71
C	SER72
C	MET104
C	ASP105
C	ZN219
C	HOH250

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	258
Details	Domain: {"description":"GST N-terminal"}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	354
Details	Domain: {"description":"GST C-terminal"}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	21
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2005","submissionDatabase":"PDB data bank","title":"Human glutathione S-transferase M1A-1A catalyzes formation of Gsh-metal complexes.","authors":["Patskovsky Y.V.","Patskovska L.N.","Listowsky I.","Almo S.C."]}},{"source":"PubMed","id":"16548513","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P10649","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	3
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P04905","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

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

Chain	Residue	Details
A	TYR6

---

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

Chain	Residue	Details
B	TYR6

---

site_id	CSA3
Number of Residues	1
Details	Annotated By Reference To The Literature 1oe8

Chain	Residue	Details
C	TYR6

---