3KAL

Structure of homoglutathione synthetase from Glycine max in closed conformation with homoglutathione, ADP, a sulfate ion, and three magnesium ions bound

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	GSH_synth_ATP	e3kalA1	A: a+b complex topology	X: Protein kinase/SAICAR synthase/ATP-grasp (From Homology)	H: Protein kinase/SAICAR synthase/ATP-grasp	T: ATP-grasp	F: GSH_synth_ATP	ECOD (1.6)
A	GSH_synthase	e3kalA2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: PreATP-grasp domain	F: GSH_synthase	ECOD (1.6)
B	GSH_synth_ATP	e3kalB1	A: a+b complex topology	X: Protein kinase/SAICAR synthase/ATP-grasp (From Homology)	H: Protein kinase/SAICAR synthase/ATP-grasp	T: ATP-grasp	F: GSH_synth_ATP	ECOD (1.6)
B	GSH_synthase	e3kalB2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: PreATP-grasp domain	F: GSH_synthase	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.1490.80	Alpha Beta	2-Layer Sandwich	Dna Ligase	domain 1	CATH (4.3.0)
A	3.30.470.20	Alpha Beta	2-Layer Sandwich	D-amino Acid Aminotransferase	Chain A, domain 1	CATH (4.3.0)
A	1.10.1080.10	Mainly Alpha	Orthogonal Bundle	Glutathione Synthetase	Chain A, domain 3	CATH (4.3.0)
A	3.40.50.1760	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glutathione synthase, substrate-binding domain superfamily, eukaryotic	CATH (4.3.0)
A	3.30.1490.50	Alpha Beta	2-Layer Sandwich	Dna Ligase	domain 1	CATH (4.3.0)
B	3.30.1490.80	Alpha Beta	2-Layer Sandwich	Dna Ligase	domain 1	CATH (4.3.0)
B	3.30.470.20	Alpha Beta	2-Layer Sandwich	D-amino Acid Aminotransferase	Chain A, domain 1	CATH (4.3.0)
B	1.10.1080.10	Mainly Alpha	Orthogonal Bundle	Glutathione Synthetase	Chain A, domain 3	CATH (4.3.0)
B	3.40.50.1760	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glutathione synthase, substrate-binding domain superfamily, eukaryotic	CATH (4.3.0)
B	3.30.1490.50	Alpha Beta	2-Layer Sandwich	Dna Ligase	domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF03917	Eukaryotic glutathione synthase, ATP binding domain (GSH_synth_ATP)	Eukaryotic glutathione synthase, ATP binding domain	-	Domain
A, B	PF03199	Eukaryotic glutathione synthase (GSH_synthase)	Eukaryotic glutathione synthase	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	homoglutathione synthetase	cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding anion binding cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding acid-amino acid ligase activity glutathione synthase activity non-ribosomal peptide synthetase activity catalytic activity ligase activity, forming carbon-nitrogen bonds ligase activity amide binding modified amino acid binding oligopeptide binding glutathione binding sulfur compound binding	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR014709	Glutathione synthase, C-terminal, eukaryotic	Homologous Superfamily
A, B	IPR016185	Pre-ATP-grasp domain superfamily	Homologous Superfamily
A, B	IPR014042	Glutathione synthase, alpha-helical	Homologous Superfamily
A, B	IPR037013	Glutathione synthase, substrate-binding domain superfamily	Homologous Superfamily
A, B	IPR014049	Glutathione synthase, N-terminal, eukaryotic	Homologous Superfamily
A, B	IPR005615	Glutathione synthase	Family
A, B	IPR004887	Glutathione synthase, substrate-binding domain	Domain

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.