2QRL

Crystal Structure of Oxalylglycine-bound Saccharopine Dehydrogenase (L-Lys Forming) from Saccharomyces cerevisiae

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	F_UNCLASSIFIED	e2qrlA1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: F_UNCLASSIFIED	ECOD (1.6)
A	PF05222	e2qrlA2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Formate/glycerate dehydrogenase catalytic domain-like	F: PF05222	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF05222	Alanine dehydrogenase/PNT, N-terminal domain (AlaDh_PNT_N)	Alanine dehydrogenase/PNT, N-terminal domain	This family now also contains the lysine 2-oxoglutarate reductases.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Saccharopine dehydrogenase, NAD+, L-lysine-forming	saccharopine dehydrogenase activity oxidoreductase activity oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor oxidoreductase activity, acting on the CH-NH group of donors catalytic activity RNA binding binding organic cyclic compound binding nucleic acid binding mRNA binding saccharopine dehydrogenase (NAD+, L-lysine-forming) activity	lysine metabolic process oxoacid metabolic process cellular biosynthetic process aspartate family amino acid biosynthetic process organonitrogen compound biosynthetic process aspartate family amino acid metabolic process amino acid metabolic process organic acid metabolic process organic acid biosynthetic process alpha-amino acid metabolic process carboxylic acid biosynthetic process lysine biosynthetic process organic substance metabolic process organic substance biosynthetic process lysine metabolic process oxoacid metabolic process cellular biosynthetic process aspartate family amino acid biosynthetic process organonitrogen compound biosynthetic process aspartate family amino acid metabolic process amino acid metabolic process organic acid metabolic process organic acid biosynthetic process alpha-amino acid metabolic process carboxylic acid biosynthetic process lysine biosynthetic process organic substance metabolic process organic substance biosynthetic process small molecule metabolic process organonitrogen compound metabolic process small molecule biosynthetic process cellular metabolic process carboxylic acid metabolic process L-amino acid biosynthetic process primary metabolic process L-amino acid metabolic process proteinogenic amino acid metabolic process amino acid biosynthetic process biosynthetic process proteinogenic amino acid biosynthetic process metabolic process cellular process alpha-amino acid biosynthetic process lysine biosynthetic process via aminoadipic acid	intracellular anatomical structure cytoplasm cellular anatomical entity membrane-bounded organelle intracellular organelle organelle peroxisome microbody intracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR007886	Alanine dehydrogenase/pyridine nucleotide transhydrogenase, N-terminal	Domain
A	IPR036291	NAD(P)-binding domain superfamily	Homologous Superfamily
A	IPR027281	Saccharopine dehydrogenase [NAD(+), L-lysine-forming]	Family
A	IPR007698	Alanine dehydrogenase/pyridine nucleotide transhydrogenase, NAD(H)-binding domain	Domain

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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 R01GM133198.