6DNA

Crystal structure of T110A mutant human Glutamate oxaloacetate transaminase 1 (GOT1)

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)
A	d6dnaa_	Alpha and beta proteins (a/b)	PLP-dependent transferase-like	PLP-dependent transferases	AAT-like	Aspartate aminotransferase, AAT	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d6dnab_	Alpha and beta proteins (a/b)	PLP-dependent transferase-like	PLP-dependent transferases	AAT-like	Aspartate aminotransferase, AAT	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d6dnac_	Alpha and beta proteins (a/b)	PLP-dependent transferase-like	PLP-dependent transferases	AAT-like	Aspartate aminotransferase, AAT	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
D	d6dnad_	Alpha and beta proteins (a/b)	PLP-dependent transferase-like	PLP-dependent transferases	AAT-like	Aspartate aminotransferase, AAT	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
E	d6dnae_	Alpha and beta proteins (a/b)	PLP-dependent transferase-like	PLP-dependent transferases	AAT-like	Aspartate aminotransferase, AAT	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
F	d6dnaf_	Alpha and beta proteins (a/b)	PLP-dependent transferase-like	PLP-dependent transferases	AAT-like	Aspartate aminotransferase, AAT	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)
A	SCOP2B Superfamily	PLP-dependent transferases	8069105	3000954	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	PLP-dependent transferases	8069105	3000954	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	PLP-dependent transferases	8069105	3000954	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	PLP-dependent transferases	8069105	3000954	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	PLP-dependent transferases	8069105	3000954	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	PLP-dependent transferases	8069105	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_1_2_C_6	e6dnaA1	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_1_2_C_6	ECOD (1.6)
A	Aminotran_1_2_N	e6dnaA2	A: a/b three-layered sandwiches	X: PLP-dependent transferases (From Topology)	H: PLP-dependent transferases (From Topology)	T: PLP-dependent transferases	F: Aminotran_1_2_N	ECOD (1.6)
B	Aminotran_1_2_C_3	e6dnaB2	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_1_2_C_3	ECOD (1.6)
B	Aminotran_1_2_N	e6dnaB1	A: a/b three-layered sandwiches	X: PLP-dependent transferases (From Topology)	H: PLP-dependent transferases (From Topology)	T: PLP-dependent transferases	F: Aminotran_1_2_N	ECOD (1.6)
C	Aminotran_1_2_C_6	e6dnaC2	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_1_2_C_6	ECOD (1.6)
C	Aminotran_1_2_N	e6dnaC1	A: a/b three-layered sandwiches	X: PLP-dependent transferases (From Topology)	H: PLP-dependent transferases (From Topology)	T: PLP-dependent transferases	F: Aminotran_1_2_N	ECOD (1.6)
D	Aminotran_1_2_C_6	e6dnaD2	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_1_2_C_6	ECOD (1.6)
D	Aminotran_1_2_N	e6dnaD1	A: a/b three-layered sandwiches	X: PLP-dependent transferases (From Topology)	H: PLP-dependent transferases (From Topology)	T: PLP-dependent transferases	F: Aminotran_1_2_N	ECOD (1.6)
E	Aminotran_1_2_C_6	e6dnaE1	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_1_2_C_6	ECOD (1.6)
E	Aminotran_1_2_N	e6dnaE2	A: a/b three-layered sandwiches	X: PLP-dependent transferases (From Topology)	H: PLP-dependent transferases (From Topology)	T: PLP-dependent transferases	F: Aminotran_1_2_N	ECOD (1.6)
F	Aminotran_1_2_C_6	e6dnaF2	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_1_2_C_6	ECOD (1.6)
F	Aminotran_1_2_N	e6dnaF1	A: a/b three-layered sandwiches	X: PLP-dependent transferases (From Topology)	H: PLP-dependent transferases (From Topology)	T: PLP-dependent transferases	F: Aminotran_1_2_N	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)
B	3.40.640.10	Alpha Beta	3-Layer(aba) Sandwich	Aspartate Aminotransferase	domain 2	CATH (4.3.0)
C	3.40.640.10	Alpha Beta	3-Layer(aba) Sandwich	Aspartate Aminotransferase	domain 2	CATH (4.3.0)
D	3.40.640.10	Alpha Beta	3-Layer(aba) Sandwich	Aspartate Aminotransferase	domain 2	CATH (4.3.0)
E	3.40.640.10	Alpha Beta	3-Layer(aba) Sandwich	Aspartate Aminotransferase	domain 2	CATH (4.3.0)
F	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, D, E A, B, C, D, E, F	PF00155	Aminotransferase class I and II (Aminotran_1_2)	Aminotransferase class I and II	-	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	Aspartate aminotransferase, cytoplasmic	transferase activity, transferring nitrogenous groups transaminase activity L-cysteine transaminase activity transferase activity catalytic activity vitamin binding vitamin B6 binding pyridoxal phosphate binding ion binding binding organic cyclic compound binding anion binding heterocyclic compound binding small molecule binding transferase activity, transferring nitrogenous groups transaminase activity L-cysteine transaminase activity transferase activity catalytic activity vitamin binding vitamin B6 binding pyridoxal phosphate binding ion binding binding organic cyclic compound binding anion binding heterocyclic compound binding small molecule binding L-aspartate:2-oxoglutarate aminotransferase activity phosphatidylserine decarboxylase activity carboxy-lyase activity lyase activity carbon-carbon lyase activity	catabolic process oxoacid metabolic process glutamine family amino acid catabolic process aspartate family amino acid metabolic process amino acid metabolic process organic acid metabolic process dicarboxylic acid catabolic process organic acid catabolic process alpha-amino acid metabolic process glutamine family amino acid metabolic process cellular catabolic process carboxylic acid catabolic process glutamate metabolic process small molecule metabolic process catabolic process oxoacid metabolic process glutamine family amino acid catabolic process aspartate family amino acid metabolic process amino acid metabolic process organic acid metabolic process dicarboxylic acid catabolic process organic acid catabolic process alpha-amino acid metabolic process glutamine family amino acid metabolic process cellular catabolic process carboxylic acid catabolic process glutamate metabolic process small molecule metabolic process aspartate metabolic process amino acid catabolic process glutamate catabolic process dicarboxylic acid metabolic process carboxylic acid metabolic process L-amino acid catabolic process primary metabolic process L-amino acid metabolic process proteinogenic amino acid metabolic process alpha-amino acid catabolic process proteinogenic amino acid catabolic process glutamate catabolic process to aspartate metabolic process cellular process small molecule catabolic process aspartate catabolic process aspartate family amino acid catabolic process carbohydrate metabolic process polyol metabolic process small molecule biosynthetic process glycerol biosynthetic process organic hydroxy compound metabolic process carbohydrate biosynthetic process alditol biosynthetic process alcohol metabolic process glycerol metabolic process biosynthetic process alditol metabolic process organic hydroxy compound biosynthetic process polyol biosynthetic process alcohol biosynthetic process response to corticosteroid response to lipid response to stimulus response to hormone response to steroid hormone response to chemical response to endogenous stimulus response to glucocorticoid response to organic cyclic compound fatty acid homeostasis chemical homeostasis homeostatic process lipid homeostasis monosaccharide metabolic process hexose metabolic process monosaccharide biosynthetic process gluconeogenesis hexose biosynthetic process glucose metabolic process aspartate family amino acid biosynthetic process organic acid biosynthetic process aspartate biosynthetic process carboxylic acid biosynthetic process dicarboxylic acid biosynthetic process L-amino acid biosynthetic process amino acid biosynthetic process proteinogenic amino acid biosynthetic process alpha-amino acid biosynthetic process cellular response to nitrogen compound cellular response to stimulus response to peptide hormone response to oxygen-containing compound cellular response to peptide hormone stimulus response to nitrogen compound cellular response to oxygen-containing compound cellular response to endogenous stimulus cellular response to chemical stimulus response to insulin cellular response to insulin stimulus cellular response to hormone stimulus 2-oxoglutarate metabolic process regulation of biological process regulation of cellular process cell surface receptor signaling pathway signaling biological regulation cell communication Notch signaling pathway signal transduction oxaloacetate metabolic process	extracellular exosome membrane-bounded organelle extracellular vesicle cellular anatomical structure extracellular organelle extracellular region organelle extracellular space vesicle extracellular membrane-bounded organelle intracellular anatomical structure cytoplasm cytosol intracellular organelle extracellular exosome membrane-bounded organelle extracellular vesicle cellular anatomical structure extracellular organelle extracellular region organelle extracellular space vesicle extracellular membrane-bounded organelle intracellular anatomical structure cytoplasm cytosol intracellular organelle nucleus intracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR004838	Aminotransferases, class-I, pyridoxal-phosphate-binding site	Binding Site
A, B, C, D, E A, B, C, D, E, F	IPR000796	Aspartate/other aminotransferase	Family
A, B, C, D, E A, B, C, D, E, F	IPR015421	Pyridoxal phosphate-dependent transferase, major domain	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR015422	Pyridoxal phosphate-dependent transferase, small domain	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR015424	Pyridoxal phosphate-dependent transferase	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR004839	Aminotransferase, class I/classII, large domain	Domain

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C, D, E A, B, C, D, E, F	Pharos: P17174	Liver Cirrhosis, Experimental malignant ependymoma medulloblastoma pancreatic ductal adenocarcinoma primitive neuroectodermal tumor adrenal cortex carcinoma subependymal giant cell astrocytoma atypical teratoid rhabdoid tumor colorectal cancer glioblastoma large cell medulloblastoma malignant glioma non-small cell lung carcinoma Pick disease rheumatoid arthritis Liver Cirrhosis, Experimental malignant ependymoma medulloblastoma pancreatic ductal adenocarcinoma primitive neuroectodermal tumor adrenal cortex carcinoma subependymal giant cell astrocytoma atypical teratoid rhabdoid tumor colorectal cancer glioblastoma large cell medulloblastoma malignant glioma non-small cell lung carcinoma Pick disease rheumatoid arthritis ankylosing spondylitis tuberculosis Crohn disease drug-induced liver injury Hashimoto thyroiditis hypothyroidism malignant mesothelioma oligodendroglioma pilocytic astrocytoma Sjogren syndrome astrocytic tumor ulcerative colitis gastric carcinoma inflammatory bowel disease

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.