2COG

Crystal structure of oxidized human cytosolic branched-chain aminotransferase complexed with 4-methylvalerate

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	d2cogb_	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	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A	d2coga_	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	automated matches	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	SCOP2 Family	D-aminoacid aminotransferase-like PLP-dependent enzymes	8062668	4002874	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	D-aminoacid aminotransferase-like PLP-dependent enzymes	8062669	3001836	SCOP2 (2022-06-29)
A	SCOP2B Superfamily	D-aminoacid aminotransferase-like PLP-dependent enzymes	8062669	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	e2cogB4	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	e2cogB3	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	e2cogA4	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	e2cogA3	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 aminotransferase 1, cytosolic	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 mitotic cell cycle process cell cycle phase transition cell cycle G1/S transition of mitotic cell cycle cell cycle G1/S phase transition mitotic cell cycle mitotic cell cycle phase transition cell cycle process lipid metabolic process L-valine biosynthetic process valine metabolic process	membrane-bounded organelle intracellular organelle intracellular anatomical structure mitochondrion organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle cytosol

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: P54687	Weight Gain cholestasis medulloblastoma osteosarcoma pancreatic intraductal papillary-mucinous carcinoma pilocytic astrocytoma Sjogren syndrome adenoma B-cell chronic lymphocytic leukemia chronic obstructive pulmonary disease exocrine pancreatic carcinoma head and neck cancer large cell medulloblastoma malignant glioma non-small cell lung carcinoma Weight Gain cholestasis medulloblastoma osteosarcoma pancreatic intraductal papillary-mucinous carcinoma pilocytic astrocytoma Sjogren syndrome adenoma B-cell chronic lymphocytic leukemia chronic obstructive pulmonary disease exocrine pancreatic carcinoma head and neck cancer large cell medulloblastoma malignant glioma non-small cell lung carcinoma ovarian cancer pancreatic intraductal papillary-mucinous neoplasm pituitary cancer tuberculosis astrocytic tumor breast cancer cystic fibrosis gastric carcinoma IgA glomerulonephritis lung carcinoma malignant pancreatic neoplasm oligodendroglioma pancreatic ductal adenocarcinoma pancreatic intraductal papillary-mucinous neoplasm with low grade dysplasia polycystic ovary syndrome ulcerative colitis atypical teratoid rhabdoid tumor Duchenne muscular dystrophy glioblastoma invasive ductal breast carcinoma malignant ependymoma

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.