2I6U

Crystal Structure of Ornithine Carbamoyltransferase complexed with Carbamoyl Phosphate and L-Norvaline from Mycobacterium tuberculosis (Rv1656) at 2.2 A

External Resource: Annotation

Domain Annotation: SCOP/SCOPe 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	d2i6ua1	Alpha and beta proteins (a/b)	ATC-like	Aspartate/ornithine carbamoyltransferase	automated matches	automated matches	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
A	d2i6ua3	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
C	d2i6uc1	Alpha and beta proteins (a/b)	ATC-like	Aspartate/ornithine carbamoyltransferase	automated matches	automated matches	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
C	d2i6uc3	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
B	d2i6ub1	Alpha and beta proteins (a/b)	ATC-like	Aspartate/ornithine carbamoyltransferase	automated matches	automated matches	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
B	d2i6ub3	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	OTCace	e2i6uA1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Aspartate/ornithine carbamoyltransferase	F: OTCace	ECOD (1.6)
A	OTCace_N	e2i6uA2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Aspartate/ornithine carbamoyltransferase	F: OTCace_N	ECOD (1.6)
C	OTCace	e2i6uC1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Aspartate/ornithine carbamoyltransferase	F: OTCace	ECOD (1.6)
C	OTCace_N	e2i6uC2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Aspartate/ornithine carbamoyltransferase	F: OTCace_N	ECOD (1.6)
B	OTCace	e2i6uB1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Aspartate/ornithine carbamoyltransferase	F: OTCace	ECOD (1.6)
B	OTCace_N	e2i6uB2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Aspartate/ornithine carbamoyltransferase	F: OTCace_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.1370	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Aspartate/ornithine carbamoyltransferase	CATH (4.3.0)
C	3.40.50.1370	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Aspartate/ornithine carbamoyltransferase	CATH (4.3.0)
B	3.40.50.1370	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Aspartate/ornithine carbamoyltransferase	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C	PF02729	Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain (OTCace_N)	Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain	-	Domain
A, B, C	PF00185	Aspartate/ornithine carbamoyltransferase, Asp/Orn binding domain (OTCace)	Aspartate/ornithine carbamoyltransferase, Asp/Orn binding domain	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	Ornithine carbamoyltransferase	binding amino acid binding carboxyl- or carbamoyltransferase activity ornithine carbamoyltransferase activity transferase activity, transferring one-carbon groups transferase activity catalytic activity	L-arginine biosynthetic process oxoacid metabolic process glutamine 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 glutamine family amino acid metabolic process arginine metabolic process small molecule metabolic process small molecule biosynthetic process carboxylic acid metabolic process primary metabolic process L-arginine biosynthetic process oxoacid metabolic process glutamine 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 glutamine family amino acid metabolic process arginine metabolic process small molecule metabolic 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 ornithine metabolic process arginine biosynthetic process via ornithine non-proteinogenic amino acid metabolic process citrulline biosynthetic process citrulline metabolic process non-proteinogenic amino acid biosynthetic process	cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR006132	Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding	Domain
A, B, C	IPR006131	Aspartate/ornithine carbamoyltransferase, Asp/Orn-binding domain	Domain
A, B, C	IPR036901	Aspartate/ornithine carbamoyltransferase superfamily	Homologous Superfamily
A, B, C	IPR006130	Aspartate/ornithine carbamoyltransferase	Family
A, B, C	IPR002292	Ornithine/putrescine carbamoyltransferase	Family
A, B, C	IPR024904	Ornithine carbamoyltransferase	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.