2F3M

Structure of human GLUTATHIONE S-TRANSFERASE M1A-1A complexed with 1-(S-(GLUTATHIONYL)-2,4,6-TRINITROCYCLOHEXADIENATE ANION

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	0042802	molecular_function	identical protein binding
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	0042802	molecular_function	identical protein binding
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	0042802	molecular_function	identical protein binding
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
D	0004364	molecular_function	glutathione transferase activity
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006629	biological_process	lipid metabolic process
D	0006693	biological_process	prostaglandin metabolic process
D	0006749	biological_process	glutathione metabolic process
D	0016740	molecular_function	transferase activity
D	0018916	biological_process	nitrobenzene metabolic process
D	0019899	molecular_function	enzyme binding
D	0042178	biological_process	xenobiotic catabolic process
D	0042802	molecular_function	identical protein binding
D	0042803	molecular_function	protein homodimerization activity
D	0043295	molecular_function	glutathione binding
D	0051122	biological_process	hepoxilin biosynthetic process
D	0070458	biological_process	cellular detoxification of nitrogen compound
D	1901687	biological_process	glutathione derivative biosynthetic process
E	0004364	molecular_function	glutathione transferase activity
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0006629	biological_process	lipid metabolic process
E	0006693	biological_process	prostaglandin metabolic process
E	0006749	biological_process	glutathione metabolic process
E	0016740	molecular_function	transferase activity
E	0018916	biological_process	nitrobenzene metabolic process
E	0019899	molecular_function	enzyme binding
E	0042178	biological_process	xenobiotic catabolic process
E	0042802	molecular_function	identical protein binding
E	0042803	molecular_function	protein homodimerization activity
E	0043295	molecular_function	glutathione binding
E	0051122	biological_process	hepoxilin biosynthetic process
E	0070458	biological_process	cellular detoxification of nitrogen compound
E	1901687	biological_process	glutathione derivative biosynthetic process
F	0004364	molecular_function	glutathione transferase activity
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0006629	biological_process	lipid metabolic process
F	0006693	biological_process	prostaglandin metabolic process
F	0006749	biological_process	glutathione metabolic process
F	0016740	molecular_function	transferase activity
F	0018916	biological_process	nitrobenzene metabolic process
F	0019899	molecular_function	enzyme binding
F	0042178	biological_process	xenobiotic catabolic process
F	0042802	molecular_function	identical protein binding
F	0042803	molecular_function	protein homodimerization activity
F	0043295	molecular_function	glutathione binding
F	0051122	biological_process	hepoxilin biosynthetic process
F	0070458	biological_process	cellular detoxification of nitrogen compound
F	1901687	biological_process	glutathione derivative biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	20
Details	BINDING SITE FOR RESIDUE GTD A 1218

Chain	Residue
A	TYR6
A	PRO60
A	GLN71
A	SER72
A	MET104
A	TYR115
A	PHE208
A	HOH1219
A	HOH1222
A	HOH1223
A	HOH1224
A	TRP7
B	ASP105
A	GLY11
A	LEU12
A	ARG42
A	TRP45
A	LYS49
A	ASN58
A	LEU59

---

site_id	AC2
Number of Residues	18
Details	BINDING SITE FOR RESIDUE GTD B 2218

Chain	Residue
A	ASP105
B	TYR6
B	TRP7
B	LEU12
B	ARG42
B	TRP45
B	LYS49
B	ASN58
B	LEU59
B	PRO60
B	GLN71
B	SER72
B	HIS107
B	MET108
B	TYR115
B	PHE208
B	HOH2219
B	HOH2223

---

site_id	AC3
Number of Residues	19
Details	BINDING SITE FOR RESIDUE GTD C 3218

Chain	Residue
C	TYR6
C	TRP7
C	ILE9
C	GLY11
C	LEU12
C	ARG42
C	TRP45
C	LYS49
C	ASN58
C	LEU59
C	PRO60
C	GLN71
C	SER72
C	HIS107
C	TYR115
C	PHE208
C	HOH3220
C	HOH3223
D	ASP105

---

site_id	AC4
Number of Residues	19
Details	BINDING SITE FOR RESIDUE GTD D 4218

Chain	Residue
C	ASP105
D	TYR6
D	TRP7
D	ILE9
D	GLY11
D	LEU12
D	ARG42
D	TRP45
D	LYS49
D	ASN58
D	LEU59
D	PRO60
D	GLN71
D	SER72
D	MET108
D	GLY111
D	TYR115
D	PHE208
D	HOH4224

---

site_id	AC5
Number of Residues	17
Details	BINDING SITE FOR RESIDUE GTD E 5218

Chain	Residue
E	TRP7
E	LEU12
E	ARG42
E	TRP45
E	LYS49
E	ASN58
E	LEU59
E	GLN71
E	SER72
E	MET104
E	HIS107
E	MET108
E	TYR115
E	PHE208
E	HOH5219
E	HOH5221
F	ASP105

---

site_id	AC6
Number of Residues	14
Details	BINDING SITE FOR RESIDUE GTD F 6218

Chain	Residue
F	LEU59
F	PRO60
F	GLN71
F	SER72
F	HIS107
F	MET108
F	TYR115
F	PHE208
E	ASP105
F	TRP7
F	LEU12
F	TRP45
F	LYS49
F	ASN58

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	516
Details	Domain: {"description":"GST N-terminal"}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	708
Details	Domain: {"description":"GST C-terminal"}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	42
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	6
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	6
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P10649","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	6
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

---

site_id	CSA4
Number of Residues	1
Details	Annotated By Reference To The Literature 1oe8

Chain	Residue	Details
D	TYR6

---

site_id	CSA5
Number of Residues	1
Details	Annotated By Reference To The Literature 1oe8

Chain	Residue	Details
E	TYR6

---

site_id	CSA6
Number of Residues	1
Details	Annotated By Reference To The Literature 1oe8

Chain	Residue	Details
F	TYR6

---