Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2VCT

Glutathione transferase A2-2 in complex with delta-4-andostrene-3-17- dione

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	7
Details	BINDING SITE FOR RESIDUE ASD A 1223

Chain	Residue
A	TYR9
A	GLY14
A	ARG15
A	LEU107
A	LEU108
A	PHE111
A	PHE222

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ASD B 1223

Chain	Residue
B	ARG15
B	LEU107
B	LEU108
B	PHE222
B	TYR9
B	GLY14

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ASD C 1223

Chain	Residue
C	TYR9
C	GLY14
C	ARG15
C	LEU107
C	LEU108
C	PHE111
C	PHE222

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ASD D 1223

Chain	Residue
D	TYR9
D	ILE12
D	GLY14
D	ARG15
D	PHE111
D	PHE222

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	32
Details	BINDING: BINDING => ECO:0000269\|PubMed:20083122

Chain	Residue	Details
A	TYR9
C	ARG45
C	GLN54
C	GLN67
D	TYR9
D	ARG45
D	GLN54
D	GLN67
E	TYR9
E	ARG45
E	GLN54
A	ARG45
E	GLN67
F	TYR9
F	ARG45
F	GLN54
F	GLN67
G	TYR9
G	ARG45
G	GLN54
G	GLN67
H	TYR9
A	GLN54
H	ARG45
H	GLN54
H	GLN67
A	GLN67
B	TYR9
B	ARG45
B	GLN54
B	GLN67
C	TYR9

site_id	SWS_FT_FI2
Number of Residues	8
Details	MOD_RES: N-acetylalanine => ECO:0000250\|UniProtKB:P30115

Chain	Residue	Details
A	ALA2
B	ALA2
C	ALA2
D	ALA2
E	ALA2
F	ALA2
G	ALA2
H	ALA2

site_id	SWS_FT_FI3
Number of Residues	8
Details	MOD_RES: N6-succinyllysine => ECO:0000250\|UniProtKB:P30115

Chain	Residue	Details
A	LYS4
B	LYS4
C	LYS4
D	LYS4
E	LYS4
F	LYS4
G	LYS4
H	LYS4

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)