2WRT

The 2.4 Angstrom structure of the Fasciola hepatica mu class GST, GST26

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004364	molecular_function	glutathione transferase activity
A	0005737	cellular_component	cytoplasm
A	0006749	biological_process	glutathione metabolic process
A	0016740	molecular_function	transferase activity
B	0004364	molecular_function	glutathione transferase activity
B	0005737	cellular_component	cytoplasm
B	0006749	biological_process	glutathione metabolic process
B	0016740	molecular_function	transferase activity
C	0004364	molecular_function	glutathione transferase activity
C	0005737	cellular_component	cytoplasm
C	0006749	biological_process	glutathione metabolic process
C	0016740	molecular_function	transferase activity
D	0004364	molecular_function	glutathione transferase activity
D	0005737	cellular_component	cytoplasm
D	0006749	biological_process	glutathione metabolic process
D	0016740	molecular_function	transferase activity
E	0004364	molecular_function	glutathione transferase activity
E	0005737	cellular_component	cytoplasm
E	0006749	biological_process	glutathione metabolic process
E	0016740	molecular_function	transferase activity
F	0004364	molecular_function	glutathione transferase activity
F	0005737	cellular_component	cytoplasm
F	0006749	biological_process	glutathione metabolic process
F	0016740	molecular_function	transferase activity
G	0004364	molecular_function	glutathione transferase activity
G	0005737	cellular_component	cytoplasm
G	0006749	biological_process	glutathione metabolic process
G	0016740	molecular_function	transferase activity
H	0004364	molecular_function	glutathione transferase activity
H	0005737	cellular_component	cytoplasm
H	0006749	biological_process	glutathione metabolic process
H	0016740	molecular_function	transferase activity
I	0004364	molecular_function	glutathione transferase activity
I	0005737	cellular_component	cytoplasm
I	0006749	biological_process	glutathione metabolic process
I	0016740	molecular_function	transferase activity
J	0004364	molecular_function	glutathione transferase activity
J	0005737	cellular_component	cytoplasm
J	0006749	biological_process	glutathione metabolic process
J	0016740	molecular_function	transferase activity
K	0004364	molecular_function	glutathione transferase activity
K	0005737	cellular_component	cytoplasm
K	0006749	biological_process	glutathione metabolic process
K	0016740	molecular_function	transferase activity
L	0004364	molecular_function	glutathione transferase activity
L	0005737	cellular_component	cytoplasm
L	0006749	biological_process	glutathione metabolic process
L	0016740	molecular_function	transferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL A 1219

Chain	Residue
A	PRO187
A	LYS188

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site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL B 1219

Chain	Residue
B	PRO187
B	LYS188
B	HOH2007

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site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL D 1219

Chain	Residue
D	PRO187
D	LYS188

---

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL E 1219

Chain	Residue
E	HOH2005
E	PRO187
E	LYS188

---

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL F 1219

Chain	Residue
F	PRO187
F	LYS188

---

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL G 1219

Chain	Residue
G	PRO187
G	LYS188
G	HOH2004

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site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL H 1219

Chain	Residue
B	HOH2113
H	PRO187
H	LYS188

---

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL I 1219

Chain	Residue
I	PRO187
I	LYS188

---

site_id	AC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL J 1219

Chain	Residue
J	PRO187
J	LYS188

---

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL J 1220

Chain	Residue
J	LEU13
J	SER68

---

site_id	BC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL H 1220

Chain	Residue
H	LEU13
H	SER68

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site_id	BC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL D 1220

Chain	Residue
D	LEU13
D	SER68

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	48
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P08515

Chain	Residue	Details
A	TYR7
C	TRP41
C	ASN54
C	GLN67
D	TYR7
D	TRP41
D	ASN54
D	GLN67
E	TYR7
E	TRP41
E	ASN54
A	TRP41
E	GLN67
F	TYR7
F	TRP41
F	ASN54
F	GLN67
G	TYR7
G	TRP41
G	ASN54
G	GLN67
H	TYR7
A	ASN54
H	TRP41
H	ASN54
H	GLN67
I	TYR7
I	TRP41
I	ASN54
I	GLN67
J	TYR7
J	TRP41
J	ASN54
A	GLN67
J	GLN67
K	TYR7
K	TRP41
K	ASN54
K	GLN67
L	TYR7
L	TRP41
L	ASN54
L	GLN67
B	TYR7
B	TRP41
B	ASN54
B	GLN67
C	TYR7

---

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	TYR111
J	TYR111
K	TYR111
L	TYR111
B	TYR111
C	TYR111
D	TYR111
E	TYR111
F	TYR111
G	TYR111
H	TYR111
I	TYR111

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