1EKP

CRYSTAL STRUCTURE OF HUMAN BRANCHED CHAIN AMINO ACID AMINOTRANSFERASE (MITOCHONDRIAL) COMPLEXED WITH PYRIDOXAL-5'-PHOSPHATE AT 2.5 ANGSTROMS (MONOCLINIC FORM).

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
Pharos: Disease Associations

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d1ekpb_	Multi-domain proteins (alpha and beta)	D-aminoacid aminotransferase-like PLP-dependent enzymes	D-aminoacid aminotransferase-like PLP-dependent enzymes	D-aminoacid aminotransferase-like PLP-dependent enzymes	Branched-chain aminoacid aminotransferase	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A	d1ekpa_	Multi-domain proteins (alpha and beta)	D-aminoacid aminotransferase-like PLP-dependent enzymes	D-aminoacid aminotransferase-like PLP-dependent enzymes	D-aminoacid aminotransferase-like PLP-dependent enzymes	Branched-chain aminoacid aminotransferase	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	D-aminoacid aminotransferase-like PLP-dependent enzymes	8036550	3001836	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	D-aminoacid aminotransferase-like PLP-dependent enzymes	8036550	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)
B	Aminotran_4_N	e1ekpB2	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	e1ekpB1	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)
A	Aminotran_4_N	e1ekpA2	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	e1ekpA1	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)
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)
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)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	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	BRANCHED CHAIN AMINO ACID AMINOTRANSFERASE (MITOCHONDRIAL)	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 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 carboxylic acid metabolic process pyruvate family amino acid metabolic process oxoacid metabolic process pyruvate family amino acid 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 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 catabolic process organic acid catabolic process branched-chain amino acid catabolic process cellular catabolic process alpha-amino acid catabolic process carboxylic acid catabolic process isoleucine catabolic process small molecule catabolic process isoleucine metabolic process amino acid catabolic process lipid metabolic process regulation of hormone levels biological regulation regulation of biological quality L-valine biosynthetic process valine metabolic process response to peptide response to stimulus response to chemical response to cytokine response to leukemia inhibitory factor cellular response to cytokine stimulus cellular response to leukemia inhibitory factor	membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure mitochondrion organelle cytoplasm intracellular membrane-bounded organelle nucleus membrane-enclosed lumen intracellular organelle lumen nucleoplasm organelle lumen nuclear lumen membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure mitochondrion organelle cytoplasm intracellular membrane-bounded organelle nucleus membrane-enclosed lumen intracellular organelle lumen nucleoplasm organelle lumen nuclear lumen mitochondrial matrix

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR005786	Branched-chain amino acid aminotransferase II	Family
A, B	IPR036038	Aminotransferase-like, PLP-dependent enzymes	Homologous Superfamily
A, B	IPR018300	Aminotransferase, class IV, conserved site	Conserved Site
A, B	IPR043132	Branched-chain-amino-acid aminotransferase-like, C-terminal	Homologous Superfamily
A, B	IPR043131	Branched-chain-amino-acid aminotransferase-like, N-terminal	Homologous Superfamily
A, B	IPR001544	Aminotransferase class IV	Family
A, B	IPR033939	Branched-chain aminotransferase	Family

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B	Pharos: O15382	maple syrup urine disease psoriasis pancreatic ductal adenocarcinoma precancerous condition ulcerative colitis attention deficit hyperactivity disorder, inattentive type classic maple syrup urine disease Crohn disease gallbladder disease intermediate maple syrup urine disease malignant ependymoma non-alcoholic fatty liver disease pancreatic intraductal papillary-mucinous neoplasm Precancerous Conditions Behcet disease maple syrup urine disease psoriasis pancreatic ductal adenocarcinoma precancerous condition ulcerative colitis attention deficit hyperactivity disorder, inattentive type classic maple syrup urine disease Crohn disease gallbladder disease intermediate maple syrup urine disease malignant ependymoma non-alcoholic fatty liver disease pancreatic intraductal papillary-mucinous neoplasm Precancerous Conditions Behcet disease colorectal cancer dental caries gastric carcinoma intermittent maple syrup urine disease ovarian cancer pancreatic intraductal papillary-mucinous neoplasm with low grade dysplasia cholelithiasis diabetes mellitus inflammatory bowel disease interstitial cystitis

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.