1AT1

CRYSTAL STRUCTURES OF PHOSPHONOACETAMIDE LIGATED T AND PHOSPHONOACETAMIDE AND MALONATE LIGATED R STATES OF ASPARTATE CARBAMOYLTRANSFERASE AT 2.8-ANGSTROMS RESOLUTION AND NEUTRAL P*H

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
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)
A	d1at1a1	Alpha and beta proteins (a/b)	ATC-like	Aspartate/ornithine carbamoyltransferase	Aspartate/ornithine carbamoyltransferase	Aspartate carbamoyltransferase catalytic subunit	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
C	d1at1c1	Alpha and beta proteins (a/b)	ATC-like	Aspartate/ornithine carbamoyltransferase	Aspartate/ornithine carbamoyltransferase	Aspartate carbamoyltransferase catalytic subunit	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d1at1b1	Alpha and beta proteins (a+b)	Ferredoxin-like	Aspartate carbamoyltransferase, Regulatory-chain, N-terminal domain	Aspartate carbamoyltransferase, Regulatory-chain, N-terminal domain	Aspartate carbamoyltransferase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d1at1b2	Small proteins	Rubredoxin-like	Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain	Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain	Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
D	d1at1d1	Alpha and beta proteins (a+b)	Ferredoxin-like	Aspartate carbamoyltransferase, Regulatory-chain, N-terminal domain	Aspartate carbamoyltransferase, Regulatory-chain, N-terminal domain	Aspartate carbamoyltransferase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
D	d1at1d2	Small proteins	Rubredoxin-like	Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain	Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain	Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Aspartate/ornithine carbamoyltransferase	8032839	3001396	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Aspartate/ornithine carbamoyltransferase	8032836	3001396	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Aspartate/ornithine carbamoyltransferase	8032839	3001396	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Aspartate/ornithine carbamoyltransferase	8032836	3001396	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Aspartate carbamoyltransferase Regulatory-chain N-terminal domain	8041529	3001148	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Aspartate carbamoyltransferase Regulatory-chain C-terminal domain	8041534	3001307	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Aspartate carbamoyltransferase Regulatory-chain C-terminal domain	8041534	3001307	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Aspartate carbamoyltransferase Regulatory-chain N-terminal domain	8041529	3001148	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	PF00185	e1at1A1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Aspartate/ornithine carbamoyltransferase	F: PF00185	ECOD (1.6)
A	PF02729	e1at1A2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Aspartate/ornithine carbamoyltransferase	F: PF02729	ECOD (1.6)
C	PF00185	e1at1C1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Aspartate/ornithine carbamoyltransferase	F: PF00185	ECOD (1.6)
C	PF02729	e1at1C2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Aspartate/ornithine carbamoyltransferase	F: PF02729	ECOD (1.6)
B	PF01948	e1at1B1	A: a+b two layers	X: Alpha-beta plaits	H: Aspartate carbamoyltransferase, Regulatory-chain, N-terminal domain (From Topology)	T: Aspartate carbamoyltransferase, Regulatory-chain, N-terminal domain	F: PF01948	ECOD (1.6)
B	PF02748	e1at1B2	A: few secondary structure elements	X: Rubredoxin-like	H: Rubredoxin-related	T: Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain	F: PF02748	ECOD (1.6)
D	PF01948	e1at1D1	A: a+b two layers	X: Alpha-beta plaits	H: Aspartate carbamoyltransferase, Regulatory-chain, N-terminal domain (From Topology)	T: Aspartate carbamoyltransferase, Regulatory-chain, N-terminal domain	F: PF01948	ECOD (1.6)
D	PF02748	e1at1D2	A: few secondary structure elements	X: Rubredoxin-like	H: Rubredoxin-related	T: Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain	F: PF02748	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	3.30.70.140	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Aspartate carbamoyltransferase regulatory subunit, N-terminal domain	CATH (4.3.0)
B	2.30.30.20	Mainly Beta	Roll	SH3 type barrels.	Aspartate carbamoyltransferase regulatory subunit, C-terminal domain	CATH (4.3.0)
D	3.30.70.140	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Aspartate carbamoyltransferase regulatory subunit, N-terminal domain	CATH (4.3.0)
D	2.30.30.20	Mainly Beta	Roll	SH3 type barrels.	Aspartate carbamoyltransferase regulatory subunit, C-terminal domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, C	PF02729	Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain (OTCace_N)	Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain	-	Domain
A, C	PF00185	Aspartate/ornithine carbamoyltransferase, Asp/Orn binding domain (OTCace)	Aspartate/ornithine carbamoyltransferase, Asp/Orn binding domain	-	Domain
B, D	PF02748	Aspartate carbamoyltransferase regulatory chain, metal binding domain (PyrI_C)	Aspartate carbamoyltransferase regulatory chain, metal binding domain	The regulatory chain is involved in allosteric regulation of aspartate carbamoyltransferase. The C-terminal metal binding domain has a rubredoxin-like fold and provides the interface with the catalytic chain.	Domain
B, D	PF01948	Aspartate carbamoyltransferase regulatory chain, allosteric domain (PyrI)	Aspartate carbamoyltransferase regulatory chain, allosteric domain	The regulatory chain is involved in allosteric regulation of aspartate carbamoyltransferase. The N-terminal domain has ferredoxin-like fold, and provides the regulatory chain dimerisation interface.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, C	ASPARTATE CARBAMOYLTRANSFERASE, CATALYTIC CHAIN	aspartate carbamoyltransferase activity carboxyl- or carbamoyltransferase activity transferase activity, transferring one-carbon groups transferase activity catalytic activity binding amino acid binding identical protein binding protein binding	organonitrogen compound metabolic process pyrimidine-containing compound metabolic process nucleobase biosynthetic process pyrimidine nucleobase biosynthetic process organonitrogen compound biosynthetic process primary metabolic process nucleobase-containing compound metabolic process pyrimidine nucleobase metabolic process organic cyclic compound metabolic process organic substance metabolic process biosynthetic process nucleobase-containing small molecule metabolic process nucleobase metabolic process organic cyclic compound biosynthetic process organic substance biosynthetic process organonitrogen compound metabolic process pyrimidine-containing compound metabolic process nucleobase biosynthetic process pyrimidine nucleobase biosynthetic process organonitrogen compound biosynthetic process primary metabolic process nucleobase-containing compound metabolic process pyrimidine nucleobase metabolic process organic cyclic compound metabolic process organic substance metabolic process biosynthetic process nucleobase-containing small molecule metabolic process nucleobase metabolic process organic cyclic compound biosynthetic process organic substance biosynthetic process 'de novo' pyrimidine nucleobase biosynthetic process small molecule metabolic process metabolic process pyrimidine-containing compound biosynthetic process glutamine metabolic process oxoacid metabolic process cellular metabolic process carboxylic acid metabolic process amino acid metabolic process organic acid metabolic process alpha-amino acid metabolic process L-amino acid metabolic process glutamine family amino acid metabolic process proteinogenic amino acid metabolic process cellular process protein-containing complex organization protein trimerization cellular component organization cellular component biogenesis cellular component assembly protein homotrimerization protein complex oligomerization protein-containing complex assembly protein homooligomerization cellular component organization or biogenesis ribose phosphate metabolic process nucleotide biosynthetic process carbohydrate derivative metabolic process pyrimidine nucleotide metabolic process 'de novo' UMP biosynthetic process ribonucleotide biosynthetic process UMP biosynthetic process ribonucleotide metabolic process ribonucleoside monophosphate metabolic process phosphate-containing compound metabolic process UMP metabolic process phosphorus metabolic process nucleoside monophosphate metabolic process ribose phosphate biosynthetic process pyrimidine ribonucleotide metabolic process nucleoside phosphate metabolic process carbohydrate derivative biosynthetic process pyrimidine nucleoside monophosphate metabolic process pyrimidine ribonucleoside monophosphate metabolic process nucleobase-containing compound biosynthetic process nucleotide metabolic process nucleoside monophosphate biosynthetic process pyrimidine ribonucleoside monophosphate biosynthetic process organophosphate metabolic process organophosphate biosynthetic process nucleoside phosphate biosynthetic process pyrimidine nucleoside monophosphate biosynthetic process ribonucleoside monophosphate biosynthetic process pyrimidine nucleotide biosynthetic process pyrimidine ribonucleotide biosynthetic process	protein-containing complex catalytic complex aspartate carbamoyltransferase complex transferase complex intracellular anatomical structure cytoplasm cellular anatomical entity cytosol
B, D	ASPARTATE CARBAMOYLTRANSFERASE REGULATORY CHAIN	cation binding transition metal ion binding zinc ion binding ion binding binding metal ion binding small molecule binding	organonitrogen compound metabolic process pyrimidine-containing compound metabolic process nucleobase biosynthetic process pyrimidine nucleobase biosynthetic process organonitrogen compound biosynthetic process primary metabolic process nucleobase-containing compound metabolic process pyrimidine nucleobase metabolic process organic cyclic compound metabolic process organic substance metabolic process biosynthetic process nucleobase-containing small molecule metabolic process nucleobase metabolic process organic cyclic compound biosynthetic process organic substance biosynthetic process organonitrogen compound metabolic process pyrimidine-containing compound metabolic process nucleobase biosynthetic process pyrimidine nucleobase biosynthetic process organonitrogen compound biosynthetic process primary metabolic process nucleobase-containing compound metabolic process pyrimidine nucleobase metabolic process organic cyclic compound metabolic process organic substance metabolic process biosynthetic process nucleobase-containing small molecule metabolic process nucleobase metabolic process organic cyclic compound biosynthetic process organic substance biosynthetic process 'de novo' pyrimidine nucleobase biosynthetic process small molecule metabolic process metabolic process pyrimidine-containing compound biosynthetic process nucleotide biosynthetic process pyrimidine nucleotide metabolic process phosphate-containing compound metabolic process phosphorus metabolic process nucleoside phosphate metabolic process cellular metabolic process nucleobase-containing compound biosynthetic process nucleotide metabolic process organophosphate metabolic process organophosphate biosynthetic process nucleoside phosphate biosynthetic process cellular process pyrimidine nucleotide biosynthetic process	intracellular anatomical structure cytoplasm cellular anatomical entity protein-containing complex catalytic complex aspartate carbamoyltransferase complex transferase complex

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, C	IPR006132	Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding	Domain
A, C	IPR006131	Aspartate/ornithine carbamoyltransferase, Asp/Orn-binding domain	Domain
A, C	IPR036901	Aspartate/ornithine carbamoyltransferase superfamily	Homologous Superfamily
A, C	IPR006130	Aspartate/ornithine carbamoyltransferase	Family
A, C	IPR002082	Aspartate carbamoyltransferase	Family
B, D	IPR036792	Aspartate carbamoyltransferase regulatory subunit, C-terminal domain superfamily	Homologous Superfamily
B, D	IPR036793	Aspartate carbamoyltransferase regulatory subunit, N-terminal domain superfamily	Homologous Superfamily
B, D	IPR020542	Aspartate carbamoyltransferase regulatory subunit, C-terminal	Domain
B, D	IPR020545	Aspartate carbamoyltransferase regulatory subunit, N-terminal	Domain
B, D	IPR002801	Aspartate transcarbamylase regulatory subunit	Family

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

Chains	Enzyme Name	Description	Catalytic Residues
A	aspartate carbamoyltransferase M-CSA #405	Aspartate carbamoyltransferase catalyses the formation of N-carbamoyl-L-aspartate and inorganic phosphate from carbamoyl phosphate and L-aspartate. In many prokaryotes such as E. coli this reaction is the committed step in pyrimidine biosynthesis. The E. coli protein exits as a heterododecamer (2C3:3R2) of six catalytic PyrB chains organized as two trimers (C3), and six regulatory PyrI chains organized as three dimers (R2). The PyrI chain is involved in the allosteric regulation of the catalytic reaction and binds one zinc ion. E. coli aspartate transcarbamoylase is feedback inhibited by CTP and by UTP in the presence of CTP.	Defined by 5 residues: ARG:A-54THR:A-55LYS:A_2-84ARG:A-105HIS:A-134 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 2.1.3.2 (PDB Primary Data) Search M-CSA Motif + EC 2.1.3.2

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 R01GM133198.