2OAT

ORNITHINE AMINOTRANSFERASE COMPLEXED WITH 5-FLUOROMETHYLORNITHINE

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
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)
B	d2oatb_	Alpha and beta proteins (a/b)	PLP-dependent transferase-like	PLP-dependent transferases	GABA-aminotransferase-like	Ornithine aminotransferase	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A	d2oata_	Alpha and beta proteins (a/b)	PLP-dependent transferase-like	PLP-dependent transferases	GABA-aminotransferase-like	Ornithine aminotransferase	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d2oatc_	Alpha and beta proteins (a/b)	PLP-dependent transferase-like	PLP-dependent transferases	GABA-aminotransferase-like	Ornithine 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	PLP-dependent transferases	8032385	3000954	SCOP2B (2022-06-29)
A	SCOP2 Family	GABA-aminotransferase-like	8020005	4000675	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	PLP-dependent transferases	8032385	3000954	SCOP2 (2022-06-29)
C	SCOP2B Superfamily	PLP-dependent transferases	8032385	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)
B	Aminotran_3_C	e2oatB3	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_3_C	ECOD (1.6)
B	Aminotran_3_N	e2oatB2	A: a/b three-layered sandwiches	X: PLP-dependent transferases (From Topology)	H: PLP-dependent transferases (From Topology)	T: PLP-dependent transferases	F: Aminotran_3_N	ECOD (1.6)
A	Aminotran_3_C	e2oatA3	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_3_C	ECOD (1.6)
A	Aminotran_3_N	e2oatA2	A: a/b three-layered sandwiches	X: PLP-dependent transferases (From Topology)	H: PLP-dependent transferases (From Topology)	T: PLP-dependent transferases	F: Aminotran_3_N	ECOD (1.6)
C	Aminotran_3_C	e2oatC3	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_3_C	ECOD (1.6)
C	Aminotran_3_N	e2oatC2	A: a/b three-layered sandwiches	X: PLP-dependent transferases (From Topology)	H: PLP-dependent transferases (From Topology)	T: PLP-dependent transferases	F: Aminotran_3_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	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)
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)
C	3.90.1150.10	Alpha Beta	Alpha-Beta Complex	Aspartate Aminotransferase, domain 1	Aspartate Aminotransferase, domain 1	CATH (4.3.0)
C	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, B, C	PF00202	Aminotransferase class-III (Aminotran_3)	Aminotransferase class-III	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	ORNITHINE AMINOTRANSFERASE	vitamin binding vitamin B6 binding pyridoxal phosphate binding ion binding binding organic cyclic compound binding anion binding heterocyclic compound binding small molecule binding identical protein binding protein binding transferase activity, transferring nitrogenous groups transaminase activity ornithine aminotransferase activity vitamin binding vitamin B6 binding pyridoxal phosphate binding ion binding binding organic cyclic compound binding anion binding heterocyclic compound binding small molecule binding identical protein binding protein binding transferase activity, transferring nitrogenous groups transaminase activity ornithine aminotransferase activity transferase activity catalytic activity	glutamine family amino acid biosynthetic process oxoacid metabolic process amino acid metabolic process L-proline biosynthetic process organic acid metabolic process organic acid biosynthetic process alpha-amino acid metabolic process carboxylic acid biosynthetic process glutamine family amino acid metabolic process proline metabolic process small molecule metabolic process proline biosynthetic process small molecule biosynthetic process carboxylic acid metabolic process glutamine family amino acid biosynthetic process oxoacid metabolic process amino acid metabolic process L-proline biosynthetic process organic acid metabolic process organic acid biosynthetic process alpha-amino acid metabolic process carboxylic acid biosynthetic process glutamine family amino acid metabolic process proline metabolic process small molecule metabolic process proline biosynthetic process small molecule biosynthetic process carboxylic acid metabolic process primary metabolic process L-amino acid biosynthetic process L-amino acid metabolic process proteinogenic amino acid metabolic process amino acid biosynthetic process biosynthetic process proteinogenic amino acid biosynthetic process metabolic process cellular process alpha-amino acid biosynthetic process catabolic process glutamine family amino acid catabolic process arginine catabolic process organic acid catabolic process cellular catabolic process arginine metabolic process carboxylic acid catabolic process amino acid catabolic process arginine catabolic process to proline L-amino acid catabolic process alpha-amino acid catabolic process proteinogenic amino acid catabolic process arginine catabolic process to proline via ornithine small molecule catabolic process multicellular organismal process sensory perception of light stimulus system process sensory perception nervous system process visual perception glutamate metabolic process arginine catabolic process to glutamate dicarboxylic acid metabolic process	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, C	IPR049704	Aminotransferases class-III pyridoxal-phosphate attachment site	Conserved Site
A, B, C	IPR050103	Class-III Pyridoxal-phosphate-dependent Aminotransferase	Family
A, B, C	IPR015421	Pyridoxal phosphate-dependent transferase, major domain	Homologous Superfamily
A, B, C	IPR015422	Pyridoxal phosphate-dependent transferase, small domain	Homologous Superfamily
A, B, C	IPR015424	Pyridoxal phosphate-dependent transferase	Homologous Superfamily
A, B, C	IPR005814	Aminotransferase class-III	Family
A, B, C	IPR010164	Ornithine aminotransferase	Family

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C	Pharos: P04181	ornithine aminotransferase deficiency liver cancer Liver Cirrhosis, Experimental perinatal necrotizing enterocolitis ulcerative colitis atypical teratoid rhabdoid tumor glioblastoma large cell medulloblastoma liver neoplasm medulloblastoma ovarian cancer Pick disease breast cancer lung cancer necrotizing enterocolitis ornithine aminotransferase deficiency liver cancer Liver Cirrhosis, Experimental perinatal necrotizing enterocolitis ulcerative colitis atypical teratoid rhabdoid tumor glioblastoma large cell medulloblastoma liver neoplasm medulloblastoma ovarian cancer Pick disease breast cancer lung cancer necrotizing enterocolitis pancreatic intraductal papillary-mucinous neoplasm with low grade dysplasia primitive neuroectodermal tumor dermatomyositis malignant glioma

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

Chains	Enzyme Name	Description	Catalytic Residues
A	ornithine aminotransferase M-CSA #929	Ornithine aminotransferase catalyses the conversion of L-ornithine and a 2-oxo acid to L-glutamate 5-semialdehyde and an L-amino acid. This enzyme is found in low-GC bacteria, where it is responsible for the fourth step in arginine biosynthesis, and in the mitochondrial matrix of eukaryotes, where it controls L-ornithine levels in tissues. In human hereditary ornithine aminotransferase deficiency, the elevated levels of intraocular concentrations of ornithine are responsible for gyrate atrophy, which affects the CNS and peripheral nervous system [PMID:12221166].	Defined by 3 residues: PHE:A-177ASP:A-263LYS:A-292 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 2.6.1.13 (PDB Primary Data) Search M-CSA Motif + EC 2.6.1.13

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.