1AAM

THE STRUCTURAL BASIS FOR THE ALTERED SUBSTRATE SPECIFICITY OF THE R292D ACTIVE SITE MUTANT OF ASPARTATE AMINOTRANSFERASE FROM E. COLI

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Structure Motif: Primary M-CSA Annotation

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1aama_	Alpha and beta proteins (a/b)	PLP-dependent transferase-like	PLP-dependent transferases	AAT-like	Aspartate aminotransferase, AAT	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	PLP-dependent transferases	8035818	3000954	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Aminotran_1_2_C_5	e1aamA2	A: a+b two layers	X: C-terminal domain in some PLP-dependent transferases (From Topology)	H: C-terminal domain in some PLP-dependent transferases (From Topology)	T: C-terminal domain in some PLP-dependent transferases	F: Aminotran_1_2_C_5	ECOD (1.6)
A	Aminotran_1_2_N	e1aamA3	A: a/b three-layered sandwiches	X: PLP-dependent transferases (From Topology)	H: PLP-dependent transferases (From Topology)	T: PLP-dependent transferases	F: Aminotran_1_2_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.1150.10	Alpha Beta	Alpha-Beta Complex	Aspartate Aminotransferase, domain 1	Aspartate Aminotransferase, domain 1	CATH (4.3.0)
A	3.40.640.10	Alpha Beta	3-Layer(aba) Sandwich	Aspartate Aminotransferase	domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00155	Aminotransferase class I and II (Aminotran_1_2)	Aminotransferase class I and II	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	ASPARTATE AMINOTRANSFERASE	transferase activity, transferring nitrogenous groups transaminase activity transferase activity L-aspartate:2-oxoglutarate aminotransferase activity catalytic activity identical protein binding protein binding binding protein homodimerization activity protein dimerization activity vitamin binding vitamin B6 binding pyridoxal phosphate binding ion binding transferase activity, transferring nitrogenous groups transaminase activity transferase activity L-aspartate:2-oxoglutarate aminotransferase activity catalytic activity identical protein binding protein binding binding protein homodimerization activity protein dimerization activity vitamin binding vitamin B6 binding pyridoxal phosphate binding ion binding organic cyclic compound binding anion binding heterocyclic compound binding small molecule binding aromatic-amino-acid transaminase activity L-tyrosine-2-oxoglutarate transaminase activity	oxoacid metabolic process amino acid metabolic process organic acid biosynthetic process organic acid metabolic process L-phenylalanine biosynthetic process from chorismate via phenylpyruvate alpha-amino acid metabolic process carboxylic acid biosynthetic process chorismate metabolic process small molecule metabolic process erythrose 4-phosphate/phosphoenolpyruvate family amino acid metabolic process L-phenylalanine biosynthetic process aromatic amino acid family biosynthetic process aromatic amino acid metabolic process small molecule biosynthetic process oxoacid metabolic process amino acid metabolic process organic acid biosynthetic process organic acid metabolic process L-phenylalanine biosynthetic process from chorismate via phenylpyruvate alpha-amino acid metabolic process carboxylic acid biosynthetic process chorismate metabolic process small molecule metabolic process erythrose 4-phosphate/phosphoenolpyruvate family amino acid metabolic process L-phenylalanine biosynthetic process aromatic amino acid family biosynthetic process aromatic amino acid metabolic process small molecule biosynthetic process dicarboxylic acid metabolic process carboxylic acid metabolic process primary metabolic process L-amino acid biosynthetic process L-amino acid metabolic process L-phenylalanine metabolic process aromatic amino acid family biosynthetic process, prephenate pathway proteinogenic amino acid metabolic process amino acid biosynthetic process biosynthetic process proteinogenic amino acid biosynthetic process metabolic process cellular process erythrose 4-phosphate/phosphoenolpyruvate family amino acid biosynthetic process alpha-amino acid biosynthetic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR004838	Aminotransferases, class-I, pyridoxal-phosphate-binding site	Binding Site
A	IPR015421	Pyridoxal phosphate-dependent transferase, major domain	Homologous Superfamily
A	IPR015422	Pyridoxal phosphate-dependent transferase, small domain	Homologous Superfamily
A	IPR015424	Pyridoxal phosphate-dependent transferase	Homologous Superfamily
A	IPR000796	Aspartate/other aminotransferase	Family
A	IPR004839	Aminotransferase, class I/classII, large domain	Domain

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	aspartate transaminase M-CSA #777	Aspartyl transferase is able to catalyse the PLP dependent transamination reaction between aspartate and 2-oxoglutarate, forming oxaloacetate and glutamate. It is part of the family of PLP dependent amino acid transferase enzymes which have high sequence homology and identical active site organisation, with the only difference being in the amino acid and ketoacid substrates. The enzymes all play key roles in the catabolism of amino acids as the products feed into the Krebs cycle and the Urea cycle.	Defined by 3 residues: TRP:A-130 [auth A-142]ASP:A-211 [auth A-223]LYS:A-246 [auth A-258] \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 2.6.1.1 (PDB Primary Data) Search M-CSA Motif + EC 2.6.1.1

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.