1BJO

THE STRUCTURE OF PHOSPHOSERINE AMINOTRANSFERASE FROM E. COLI IN COMPLEX WITH ALPHA-METHYL-L-GLUTAMATE

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
Protein Modification Annotation
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	d1bjoa_	Alpha and beta proteins (a/b)	PLP-dependent transferase-like	PLP-dependent transferases	GABA-aminotransferase-like	Phosphoserine aminotransferase, PSAT	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d1bjob_	Alpha and beta proteins (a/b)	PLP-dependent transferase-like	PLP-dependent transferases	GABA-aminotransferase-like	Phosphoserine aminotransferase, PSAT	(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	8032395	3000954	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	PLP-dependent transferases	8032395	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_5_C_1	e1bjoA2	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_5_C_1	ECOD (1.6)
A	UNK_F_TYPE	e1bjoA3	A: a/b three-layered sandwiches	X: PLP-dependent transferases (From Topology)	H: PLP-dependent transferases (From Topology)	T: PLP-dependent transferases	F: UNK_F_TYPE	ECOD (1.6)
B	Aminotran_5_C_1	e1bjoB2	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_5_C_1	ECOD (1.6)
B	UNK_F_TYPE	e1bjoB3	A: a/b three-layered sandwiches	X: PLP-dependent transferases (From Topology)	H: PLP-dependent transferases (From Topology)	T: PLP-dependent transferases	F: UNK_F_TYPE	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

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

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00266	Aminotransferase class-V (Aminotran_5)	Aminotransferase class-V	This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.	Domain
B	PF00266	Aminotransferase class-V (Aminotran_5)	Aminotransferase class-V	This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	PHOSPHOSERINE AMINOTRANSFERASE	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 transferase activity, transferring nitrogenous groups 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 transferase activity, transferring nitrogenous groups transaminase activity transferase activity catalytic activity O-phospho-L-serine:2-oxoglutarate aminotransferase activity	lysine metabolic process oxoacid metabolic process aspartate family amino acid 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 small molecule metabolic process small molecule biosynthetic process dicarboxylic acid metabolic process carboxylic acid metabolic process lysine metabolic process oxoacid metabolic process aspartate family amino acid 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 small molecule metabolic process small molecule biosynthetic process dicarboxylic acid metabolic process carboxylic acid metabolic process L-amino acid biosynthetic process primary metabolic process L-amino acid metabolic process diaminopimelate metabolic process fatty acid derivative metabolic process proteinogenic amino acid metabolic process amino acid biosynthetic process biosynthetic process lysine biosynthetic process via diaminopimelate lysine biosynthetic process via diaminopimelate and N-succinyl-2-amino-6-ketopimelate proteinogenic amino acid biosynthetic process metabolic process cellular process alpha-amino acid biosynthetic process lipid metabolic process organic hydroxy compound metabolic process vitamin biosynthetic process aldehyde biosynthetic process pyridoxal phosphate biosynthetic process phosphate-containing compound metabolic process pyridine-containing compound metabolic process phosphorus metabolic process water-soluble vitamin metabolic process vitamin B6 biosynthetic process water-soluble vitamin biosynthetic process pyridine-containing compound biosynthetic process aldehyde metabolic process vitamin metabolic process organophosphate metabolic process organophosphate biosynthetic process organic hydroxy compound biosynthetic process vitamin B6 metabolic process pyridoxal phosphate metabolic process pyridoxine biosynthetic process pyridoxine metabolic process serine family amino acid metabolic process L-serine metabolic process L-serine biosynthetic process serine family amino acid biosynthetic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol
B	PHOSPHOSERINE AMINOTRANSFERASE	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 transferase activity, transferring nitrogenous groups 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 transferase activity, transferring nitrogenous groups transaminase activity transferase activity catalytic activity O-phospho-L-serine:2-oxoglutarate aminotransferase activity	lysine metabolic process oxoacid metabolic process aspartate family amino acid 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 small molecule metabolic process small molecule biosynthetic process dicarboxylic acid metabolic process carboxylic acid metabolic process lysine metabolic process oxoacid metabolic process aspartate family amino acid 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 small molecule metabolic process small molecule biosynthetic process dicarboxylic acid metabolic process carboxylic acid metabolic process L-amino acid biosynthetic process primary metabolic process L-amino acid metabolic process diaminopimelate metabolic process fatty acid derivative metabolic process proteinogenic amino acid metabolic process amino acid biosynthetic process biosynthetic process lysine biosynthetic process via diaminopimelate lysine biosynthetic process via diaminopimelate and N-succinyl-2-amino-6-ketopimelate proteinogenic amino acid biosynthetic process metabolic process cellular process alpha-amino acid biosynthetic process lipid metabolic process organic hydroxy compound metabolic process vitamin biosynthetic process aldehyde biosynthetic process pyridoxal phosphate biosynthetic process phosphate-containing compound metabolic process pyridine-containing compound metabolic process phosphorus metabolic process water-soluble vitamin metabolic process vitamin B6 biosynthetic process water-soluble vitamin biosynthetic process pyridine-containing compound biosynthetic process aldehyde metabolic process vitamin metabolic process organophosphate metabolic process organophosphate biosynthetic process organic hydroxy compound biosynthetic process vitamin B6 metabolic process pyridoxal phosphate metabolic process pyridoxine biosynthetic process pyridoxine metabolic process serine family amino acid metabolic process L-serine metabolic process L-serine biosynthetic process serine family amino acid biosynthetic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR020578	Aminotransferase class-V, 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	IPR022278	Phosphoserine aminotransferase	Family
A	IPR015424	Pyridoxal phosphate-dependent transferase	Homologous Superfamily
A	IPR000192	Aminotransferase class V domain	Domain
B	IPR020578	Aminotransferase class-V, pyridoxal-phosphate binding site	Binding Site
B	IPR015421	Pyridoxal phosphate-dependent transferase, major domain	Homologous Superfamily
B	IPR015422	Pyridoxal phosphate-dependent transferase, small domain	Homologous Superfamily
B	IPR022278	Phosphoserine aminotransferase	Family
B	IPR015424	Pyridoxal phosphate-dependent transferase	Homologous Superfamily
B	IPR000192	Aminotransferase class V domain	Domain

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
B	LLP	Parent Component: LYS RESID: AA0119 PSI-MOD : N6-pyridoxal phosphate-L-lysine MOD:00128

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

Chains	Enzyme Name	Description	Catalytic Residues
A	phosphoserine transaminase M-CSA #424	A pyridoxal-phosphate-dependent enzyme. It catalyses the second step in the phosphorylated pathway of serine biosynthesis in Escherichia coli (the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine). It also catalyses the third step in the biosynthesis of the coenzyme pyridoxal 5'-phosphate in E. coli (the reversible conversion of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine).	Defined by 3 residues: TRP:A-100 [auth A-102]ASP:A-172 [auth A-174]LYS:A-196 [auth A-198] \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 2.6.1.52 (PDB Primary Data) Search M-CSA Motif + EC 2.6.1.52

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.