Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1GUH

Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the MU and PI class enzymes

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004364	molecular_function	glutathione transferase activity
A	0004601	molecular_function	peroxidase activity
A	0004602	molecular_function	glutathione peroxidase activity
A	0004769	molecular_function	steroid delta-isomerase activity
A	0005504	molecular_function	fatty acid binding
A	0005515	molecular_function	protein binding
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	0006805	biological_process	xenobiotic metabolic process
A	0016740	molecular_function	transferase activity
A	0016853	molecular_function	isomerase activity
A	0030855	biological_process	epithelial cell differentiation
A	0043651	biological_process	linoleic acid metabolic process
A	0070062	cellular_component	extracellular exosome
A	0098869	biological_process	cellular oxidant detoxification
A	1901687	biological_process	glutathione derivative biosynthetic process
B	0004364	molecular_function	glutathione transferase activity
B	0004601	molecular_function	peroxidase activity
B	0004602	molecular_function	glutathione peroxidase activity
B	0004769	molecular_function	steroid delta-isomerase activity
B	0005504	molecular_function	fatty acid binding
B	0005515	molecular_function	protein binding
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	0006805	biological_process	xenobiotic metabolic process
B	0016740	molecular_function	transferase activity
B	0016853	molecular_function	isomerase activity
B	0030855	biological_process	epithelial cell differentiation
B	0043651	biological_process	linoleic acid metabolic process
B	0070062	cellular_component	extracellular exosome
B	0098869	biological_process	cellular oxidant detoxification
B	1901687	biological_process	glutathione derivative biosynthetic process
C	0004364	molecular_function	glutathione transferase activity
C	0004601	molecular_function	peroxidase activity
C	0004602	molecular_function	glutathione peroxidase activity
C	0004769	molecular_function	steroid delta-isomerase activity
C	0005504	molecular_function	fatty acid binding
C	0005515	molecular_function	protein binding
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	0006805	biological_process	xenobiotic metabolic process
C	0016740	molecular_function	transferase activity
C	0016853	molecular_function	isomerase activity
C	0030855	biological_process	epithelial cell differentiation
C	0043651	biological_process	linoleic acid metabolic process
C	0070062	cellular_component	extracellular exosome
C	0098869	biological_process	cellular oxidant detoxification
C	1901687	biological_process	glutathione derivative biosynthetic process
D	0004364	molecular_function	glutathione transferase activity
D	0004601	molecular_function	peroxidase activity
D	0004602	molecular_function	glutathione peroxidase activity
D	0004769	molecular_function	steroid delta-isomerase activity
D	0005504	molecular_function	fatty acid binding
D	0005515	molecular_function	protein binding
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	0006805	biological_process	xenobiotic metabolic process
D	0016740	molecular_function	transferase activity
D	0016853	molecular_function	isomerase activity
D	0030855	biological_process	epithelial cell differentiation
D	0043651	biological_process	linoleic acid metabolic process
D	0070062	cellular_component	extracellular exosome
D	0098869	biological_process	cellular oxidant detoxification
D	1901687	biological_process	glutathione derivative biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GSB A 223

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

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GSB B 223

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

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GSB C 223

Chain	Residue
C	TYR9
C	ARG45
C	GLN54
C	VAL55
C	PRO56
C	GLN67
C	THR68
D	ASP101
D	ARG131

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GSB D 223

Chain	Residue
C	ASP101
C	ARG131
D	TYR9
D	ARG45
D	GLN54
D	VAL55
D	PRO56
D	GLN67
D	THR68

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	BINDING: BINDING => ECO:0000269\|PubMed:16421451, ECO:0000269\|PubMed:19618965

Chain	Residue	Details
A	PHE10
C	ASN46
C	VAL55
C	THR68
D	PHE10
D	ASN46
D	VAL55
D	THR68
A	ASN46
A	VAL55
A	THR68
B	PHE10
B	ASN46
B	VAL55
B	THR68
C	PHE10

site_id	SWS_FT_FI2
Number of Residues	4
Details	MOD_RES: N-acetylmethionine => ECO:0000250\|UniProtKB:P80894

Chain	Residue	Details
A	ALA2
B	ALA2
C	ALA2
D	ALA2

site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: N-acetylalanine; in Glutathione S-transferase A1, N-terminally processed => ECO:0000250\|UniProtKB:P30115

Chain	Residue	Details
A	GLU3
B	GLU3
C	GLU3
D	GLU3

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: N6-succinyllysine => ECO:0000250\|UniProtKB:P30115

Chain	Residue	Details
A	PRO5
B	PRO5
C	PRO5
D	PRO5

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

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