2EJ0

Crystal Structure of T.th.HB8 Branched-Chain Amino Acid Aminotransferase with Pyridoxamine 5'-phosphate

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

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d2ej0a_	Multi-domain proteins (alpha and beta)	D-aminoacid aminotransferase-like PLP-dependent enzymes	D-aminoacid aminotransferase-like PLP-dependent enzymes	automated matches	automated matches	(Thermus thermophilus HB8 ) [TaxId: 300852 ],	SCOPe (2.08)
E	d2ej0e_	Multi-domain proteins (alpha and beta)	D-aminoacid aminotransferase-like PLP-dependent enzymes	D-aminoacid aminotransferase-like PLP-dependent enzymes	automated matches	automated matches	(Thermus thermophilus HB8 ) [TaxId: 300852 ],	SCOPe (2.08)
B	d2ej0b_	Multi-domain proteins (alpha and beta)	D-aminoacid aminotransferase-like PLP-dependent enzymes	D-aminoacid aminotransferase-like PLP-dependent enzymes	automated matches	automated matches	(Thermus thermophilus HB8 ) [TaxId: 300852 ],	SCOPe (2.08)
C	d2ej0c_	Multi-domain proteins (alpha and beta)	D-aminoacid aminotransferase-like PLP-dependent enzymes	D-aminoacid aminotransferase-like PLP-dependent enzymes	automated matches	automated matches	(Thermus thermophilus HB8 ) [TaxId: 300852 ],	SCOPe (2.08)
D	d2ej0d_	Multi-domain proteins (alpha and beta)	D-aminoacid aminotransferase-like PLP-dependent enzymes	D-aminoacid aminotransferase-like PLP-dependent enzymes	automated matches	automated matches	(Thermus thermophilus HB8 ) [TaxId: 300852 ],	SCOPe (2.08)
F	d2ej0f_	Multi-domain proteins (alpha and beta)	D-aminoacid aminotransferase-like PLP-dependent enzymes	D-aminoacid aminotransferase-like PLP-dependent enzymes	automated matches	automated matches	(Thermus thermophilus HB8 ) [TaxId: 300852 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	D-aminoacid aminotransferase-like PLP-dependent enzymes	8075704	3001836	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	D-aminoacid aminotransferase-like PLP-dependent enzymes	8075704	3001836	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	D-aminoacid aminotransferase-like PLP-dependent enzymes	8075704	3001836	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	D-aminoacid aminotransferase-like PLP-dependent enzymes	8075704	3001836	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	D-aminoacid aminotransferase-like PLP-dependent enzymes	8075704	3001836	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	D-aminoacid aminotransferase-like PLP-dependent enzymes	8075704	3001836	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_4_N	e2ej0A2	A: a+b two layers	X: a+b domain in D-aminoacid aminotransferase-like PLP-dependent enzymes (From Topology)	H: a+b domain in D-aminoacid aminotransferase-like PLP-dependent enzymes (From Topology)	T: a+b domain in D-aminoacid aminotransferase-like PLP-dependent enzymes	F: Aminotran_4_N	ECOD (1.6)
A	Aminotran_4_C	e2ej0A1	A: a+b two layers	X: barrel domain in D-aminoacid aminotransferase-like PLP-dependent enzymes (From Topology)	H: barrel domain in D-aminoacid aminotransferase-like PLP-dependent enzymes (From Topology)	T: barrel domain in D-aminoacid aminotransferase-like PLP-dependent enzymes	F: Aminotran_4_C	ECOD (1.6)
E	Aminotran_4_N	e2ej0E1	A: a+b two layers	X: a+b domain in D-aminoacid aminotransferase-like PLP-dependent enzymes (From Topology)	H: a+b domain in D-aminoacid aminotransferase-like PLP-dependent enzymes (From Topology)	T: a+b domain in D-aminoacid aminotransferase-like PLP-dependent enzymes	F: Aminotran_4_N	ECOD (1.6)
E	Aminotran_4_C	e2ej0E2	A: a+b two layers	X: barrel domain in D-aminoacid aminotransferase-like PLP-dependent enzymes (From Topology)	H: barrel domain in D-aminoacid aminotransferase-like PLP-dependent enzymes (From Topology)	T: barrel domain in D-aminoacid aminotransferase-like PLP-dependent enzymes	F: Aminotran_4_C	ECOD (1.6)
B	Aminotran_4_N	e2ej0B2	A: a+b two layers	X: a+b domain in D-aminoacid aminotransferase-like PLP-dependent enzymes (From Topology)	H: a+b domain in D-aminoacid aminotransferase-like PLP-dependent enzymes (From Topology)	T: a+b domain in D-aminoacid aminotransferase-like PLP-dependent enzymes	F: Aminotran_4_N	ECOD (1.6)
B	Aminotran_4_C	e2ej0B1	A: a+b two layers	X: barrel domain in D-aminoacid aminotransferase-like PLP-dependent enzymes (From Topology)	H: barrel domain in D-aminoacid aminotransferase-like PLP-dependent enzymes (From Topology)	T: barrel domain in D-aminoacid aminotransferase-like PLP-dependent enzymes	F: Aminotran_4_C	ECOD (1.6)
C	Aminotran_4_N	e2ej0C2	A: a+b two layers	X: a+b domain in D-aminoacid aminotransferase-like PLP-dependent enzymes (From Topology)	H: a+b domain in D-aminoacid aminotransferase-like PLP-dependent enzymes (From Topology)	T: a+b domain in D-aminoacid aminotransferase-like PLP-dependent enzymes	F: Aminotran_4_N	ECOD (1.6)
C	Aminotran_4_C	e2ej0C1	A: a+b two layers	X: barrel domain in D-aminoacid aminotransferase-like PLP-dependent enzymes (From Topology)	H: barrel domain in D-aminoacid aminotransferase-like PLP-dependent enzymes (From Topology)	T: barrel domain in D-aminoacid aminotransferase-like PLP-dependent enzymes	F: Aminotran_4_C	ECOD (1.6)
D	Aminotran_4_N	e2ej0D2	A: a+b two layers	X: a+b domain in D-aminoacid aminotransferase-like PLP-dependent enzymes (From Topology)	H: a+b domain in D-aminoacid aminotransferase-like PLP-dependent enzymes (From Topology)	T: a+b domain in D-aminoacid aminotransferase-like PLP-dependent enzymes	F: Aminotran_4_N	ECOD (1.6)
D	Aminotran_4_C	e2ej0D1	A: a+b two layers	X: barrel domain in D-aminoacid aminotransferase-like PLP-dependent enzymes (From Topology)	H: barrel domain in D-aminoacid aminotransferase-like PLP-dependent enzymes (From Topology)	T: barrel domain in D-aminoacid aminotransferase-like PLP-dependent enzymes	F: Aminotran_4_C	ECOD (1.6)
F	Aminotran_4_N	e2ej0F2	A: a+b two layers	X: a+b domain in D-aminoacid aminotransferase-like PLP-dependent enzymes (From Topology)	H: a+b domain in D-aminoacid aminotransferase-like PLP-dependent enzymes (From Topology)	T: a+b domain in D-aminoacid aminotransferase-like PLP-dependent enzymes	F: Aminotran_4_N	ECOD (1.6)
F	Aminotran_4_C	e2ej0F1	A: a+b two layers	X: barrel domain in D-aminoacid aminotransferase-like PLP-dependent enzymes (From Topology)	H: barrel domain in D-aminoacid aminotransferase-like PLP-dependent enzymes (From Topology)	T: barrel domain in D-aminoacid aminotransferase-like PLP-dependent enzymes	F: Aminotran_4_C	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.470.10	Alpha Beta	2-Layer Sandwich	D-amino Acid Aminotransferase	Chain A, domain 1	CATH (4.3.0)
A	3.20.10.10	Alpha Beta	Alpha-Beta Barrel	D-amino Acid Aminotransferase	Chain A, domain 2	CATH (4.3.0)
E	3.30.470.10	Alpha Beta	2-Layer Sandwich	D-amino Acid Aminotransferase	Chain A, domain 1	CATH (4.3.0)
E	3.20.10.10	Alpha Beta	Alpha-Beta Barrel	D-amino Acid Aminotransferase	Chain A, domain 2	CATH (4.3.0)
B	3.30.470.10	Alpha Beta	2-Layer Sandwich	D-amino Acid Aminotransferase	Chain A, domain 1	CATH (4.3.0)
B	3.20.10.10	Alpha Beta	Alpha-Beta Barrel	D-amino Acid Aminotransferase	Chain A, domain 2	CATH (4.3.0)
C	3.30.470.10	Alpha Beta	2-Layer Sandwich	D-amino Acid Aminotransferase	Chain A, domain 1	CATH (4.3.0)
C	3.20.10.10	Alpha Beta	Alpha-Beta Barrel	D-amino Acid Aminotransferase	Chain A, domain 2	CATH (4.3.0)
D	3.30.470.10	Alpha Beta	2-Layer Sandwich	D-amino Acid Aminotransferase	Chain A, domain 1	CATH (4.3.0)
D	3.20.10.10	Alpha Beta	Alpha-Beta Barrel	D-amino Acid Aminotransferase	Chain A, domain 2	CATH (4.3.0)
F	3.30.470.10	Alpha Beta	2-Layer Sandwich	D-amino Acid Aminotransferase	Chain A, domain 1	CATH (4.3.0)
F	3.20.10.10	Alpha Beta	Alpha-Beta Barrel	D-amino Acid Aminotransferase	Chain A, domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F	PF01063	Amino-transferase class IV (Aminotran_4)	Amino-transferase class IV	The D-amino acid transferases (D-AAT) are required by bacteria to catalyse the synthesis of D-glutamic acid and D-alanine, which are essential constituents of bacterial cell wall and are the building block for other D-amino acids. Despite the diff ...	The D-amino acid transferases (D-AAT) are required by bacteria to catalyse the synthesis of D-glutamic acid and D-alanine, which are essential constituents of bacterial cell wall and are the building block for other D-amino acids. Despite the difference in the structure of the substrates, D-AATs and L-ATTs have strong similarity.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F	Branched-chain amino acid aminotransferase	transferase activity, transferring nitrogenous groups branched-chain-amino-acid transaminase activity transaminase activity L-leucine-2-oxoglutarate transaminase activity transferase activity catalytic activity L-valine-2-oxoglutarate transaminase activity L-isoleucine-2-oxoglutarate transaminase activity	pyruvate family amino acid metabolic process oxoacid metabolic process pyruvate family amino acid biosynthetic process cellular biosynthetic process amino acid metabolic process organic acid metabolic process organic acid biosynthetic process alpha-amino acid metabolic process carboxylic acid biosynthetic process small molecule metabolic process branched-chain amino acid metabolic process L-leucine metabolic process L-leucine biosynthetic process small molecule biosynthetic process pyruvate family amino acid metabolic process oxoacid metabolic process pyruvate family amino acid biosynthetic process cellular biosynthetic process amino acid metabolic process organic acid metabolic process organic acid biosynthetic process alpha-amino acid metabolic process carboxylic acid biosynthetic process small molecule metabolic process branched-chain amino acid metabolic process L-leucine metabolic process L-leucine biosynthetic 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 branched-chain amino acid biosynthetic process proteinogenic amino acid biosynthetic process metabolic process cellular process alpha-amino acid biosynthetic process isoleucine biosynthetic process isoleucine metabolic process L-valine biosynthetic process valine metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR005785	Branched-chain amino acid aminotransferase I	Family
A, B, C, D, E A, B, C, D, E, F	IPR050571	Class-IV Pyridoxal-Phosphate-Dependent Aminotransferase	Family
A, B, C, D, E A, B, C, D, E, F	IPR036038	Aminotransferase-like, PLP-dependent enzymes	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR043132	Branched-chain-amino-acid aminotransferase-like, C-terminal	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR043131	Branched-chain-amino-acid aminotransferase-like, N-terminal	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR001544	Aminotransferase class IV	Family
A, B, C, D, E A, B, C, D, E, F	IPR033939	Branched-chain aminotransferase	Family

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.