Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2WJU

Glutathione transferase A2-2 in complex with glutathione

Replaces: 2VCR

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	0006805	biological_process	xenobiotic metabolic process
A	0016740	molecular_function	transferase activity
A	0030855	biological_process	epithelial cell differentiation
A	0070062	cellular_component	extracellular exosome
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	0006805	biological_process	xenobiotic metabolic process
B	0016740	molecular_function	transferase activity
B	0030855	biological_process	epithelial cell differentiation
B	0070062	cellular_component	extracellular exosome
C	0004364	molecular_function	glutathione transferase activity
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006749	biological_process	glutathione metabolic process
C	0006805	biological_process	xenobiotic metabolic process
C	0016740	molecular_function	transferase activity
C	0030855	biological_process	epithelial cell differentiation
C	0070062	cellular_component	extracellular exosome
D	0004364	molecular_function	glutathione transferase activity
D	0005515	molecular_function	protein binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006749	biological_process	glutathione metabolic process
D	0006805	biological_process	xenobiotic metabolic process
D	0016740	molecular_function	transferase activity
D	0030855	biological_process	epithelial cell differentiation
D	0070062	cellular_component	extracellular exosome
E	0004364	molecular_function	glutathione transferase activity
E	0005515	molecular_function	protein binding
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0006749	biological_process	glutathione metabolic process
E	0006805	biological_process	xenobiotic metabolic process
E	0016740	molecular_function	transferase activity
E	0030855	biological_process	epithelial cell differentiation
E	0070062	cellular_component	extracellular exosome
F	0004364	molecular_function	glutathione transferase activity
F	0005515	molecular_function	protein binding
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0006749	biological_process	glutathione metabolic process
F	0006805	biological_process	xenobiotic metabolic process
F	0016740	molecular_function	transferase activity
F	0030855	biological_process	epithelial cell differentiation
F	0070062	cellular_component	extracellular exosome
G	0004364	molecular_function	glutathione transferase activity
G	0005515	molecular_function	protein binding
G	0005737	cellular_component	cytoplasm
G	0005829	cellular_component	cytosol
G	0006749	biological_process	glutathione metabolic process
G	0006805	biological_process	xenobiotic metabolic process
G	0016740	molecular_function	transferase activity
G	0030855	biological_process	epithelial cell differentiation
G	0070062	cellular_component	extracellular exosome
H	0004364	molecular_function	glutathione transferase activity
H	0005515	molecular_function	protein binding
H	0005737	cellular_component	cytoplasm
H	0005829	cellular_component	cytosol
H	0006749	biological_process	glutathione metabolic process
H	0006805	biological_process	xenobiotic metabolic process
H	0016740	molecular_function	transferase activity
H	0030855	biological_process	epithelial cell differentiation
H	0070062	cellular_component	extracellular exosome

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE GSH A 230

Chain	Residue
A	TYR9
A	HOH2080
B	ASP101
B	ARG131
A	ARG15
A	ARG45
A	GLN54
A	VAL55
A	PRO56
A	GLN67
A	THR68
A	PHE220

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE GSH B 230

Chain	Residue
A	ASP101
A	ARG131
B	TYR9
B	ARG15
B	ARG45
B	GLN54
B	VAL55
B	GLN67
B	THR68
B	PHE220
B	HOH2090

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GSH C 230

Chain	Residue
C	ARG45
C	GLN54
C	VAL55
C	GLN67
C	THR68
C	PHE220
D	ASP101
D	ARG131

site_id	AC4
Number of Residues	13
Details	BINDING SITE FOR RESIDUE GSH D 230

Chain	Residue
C	ASP101
C	ARG131
D	TYR9
D	ARG15
D	ARG45
D	GLN54
D	VAL55
D	GLN67
D	THR68
D	PHE220
D	HOH2029
D	HOH2077
D	HOH2078

site_id	AC5
Number of Residues	12
Details	BINDING SITE FOR RESIDUE GSH E 230

Chain	Residue
E	TYR9
E	ARG45
E	GLN54
E	VAL55
E	GLN67
E	THR68
E	PHE220
E	HOH2028
E	HOH2091
E	HOH2092
F	ASP101
F	ARG131

site_id	AC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE GSH F 230

Chain	Residue
E	ASP101
E	ARG131
F	TYR9
F	ARG15
F	ARG45
F	GLN54
F	VAL55
F	GLN67
F	THR68
F	PHE220
F	HOH2016
F	HOH2017

site_id	AC7
Number of Residues	12
Details	BINDING SITE FOR RESIDUE GSH G 230

Chain	Residue
G	TYR9
G	ARG15
G	ARG45
G	GLN54
G	VAL55
G	PRO56
G	GLN67
G	THR68
G	PHE220
G	HOH2039
H	ASP101
H	ARG131

site_id	AC8
Number of Residues	12
Details	BINDING SITE FOR RESIDUE GSH H 230

Chain	Residue
G	ASP101
G	ARG131
H	TYR9
H	ARG15
H	ARG45
H	GLN53
H	GLN54
H	VAL55
H	GLN67
H	THR68
H	HOH2011
H	HOH2047

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	640
Details	Domain: {"description":"GST N-terminal"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	976
Details	Domain: {"description":"GST C-terminal"}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	184
Details	Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	128
Details	Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	32
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20083122","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	8
Details	Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"UniProtKB","id":"P30115","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	8
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P30115","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	TYR9

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

Chain	Residue	Details
B	TYR9

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

Chain	Residue	Details
C	TYR9

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

Chain	Residue	Details
D	TYR9

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

Chain	Residue	Details
E	TYR9

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

Chain	Residue	Details
F	TYR9

site_id	CSA7
Number of Residues	1
Details	Annotated By Reference To The Literature 1oe8

Chain	Residue	Details
G	TYR9

site_id	CSA8
Number of Residues	1
Details	Annotated By Reference To The Literature 1oe8

Chain	Residue	Details
H	TYR9

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)