1J1Z

Crystal Structure of Thermus thermophilus HB8 Argininosuccinate Synthetase in complex with substrate

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

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
C	d1j1zc1	Alpha and beta proteins (a/b)	Adenine nucleotide alpha hydrolase-like	Adenine nucleotide alpha hydrolases-like	N-type ATP pyrophosphatases	Argininosuccinate synthetase, N-terminal domain	(Thermus thermophilus ) [TaxId: 274 ],	SCOPe (2.08)
C	d1j1zc2	Alpha and beta proteins (a+b)	Argininosuccinate synthetase, C-terminal domain	Argininosuccinate synthetase, C-terminal domain	Argininosuccinate synthetase, C-terminal domain	Argininosuccinate synthetase, C-terminal domain	(Thermus thermophilus ) [TaxId: 274 ],	SCOPe (2.08)
D	d1j1zd1	Alpha and beta proteins (a/b)	Adenine nucleotide alpha hydrolase-like	Adenine nucleotide alpha hydrolases-like	N-type ATP pyrophosphatases	Argininosuccinate synthetase, N-terminal domain	(Thermus thermophilus ) [TaxId: 274 ],	SCOPe (2.08)
D	d1j1zd2	Alpha and beta proteins (a+b)	Argininosuccinate synthetase, C-terminal domain	Argininosuccinate synthetase, C-terminal domain	Argininosuccinate synthetase, C-terminal domain	Argininosuccinate synthetase, C-terminal domain	(Thermus thermophilus ) [TaxId: 274 ],	SCOPe (2.08)
A	d1j1za1	Alpha and beta proteins (a/b)	Adenine nucleotide alpha hydrolase-like	Adenine nucleotide alpha hydrolases-like	N-type ATP pyrophosphatases	Argininosuccinate synthetase, N-terminal domain	(Thermus thermophilus ) [TaxId: 274 ],	SCOPe (2.08)
A	d1j1za2	Alpha and beta proteins (a+b)	Argininosuccinate synthetase, C-terminal domain	Argininosuccinate synthetase, C-terminal domain	Argininosuccinate synthetase, C-terminal domain	Argininosuccinate synthetase, C-terminal domain	(Thermus thermophilus ) [TaxId: 274 ],	SCOPe (2.08)
B	d1j1zb1	Alpha and beta proteins (a/b)	Adenine nucleotide alpha hydrolase-like	Adenine nucleotide alpha hydrolases-like	N-type ATP pyrophosphatases	Argininosuccinate synthetase, N-terminal domain	(Thermus thermophilus ) [TaxId: 274 ],	SCOPe (2.08)
B	d1j1zb2	Alpha and beta proteins (a+b)	Argininosuccinate synthetase, C-terminal domain	Argininosuccinate synthetase, C-terminal domain	Argininosuccinate synthetase, C-terminal domain	Argininosuccinate synthetase, C-terminal domain	(Thermus thermophilus ) [TaxId: 274 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
C	SCOP2B Superfamily	Argininosuccinate synthetase, C-terminal domain	8032266	3001063	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Adenine nucleotide alpha hydrolases-like	8032265	3001593	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Argininosuccinate synthetase, C-terminal domain	8032266	3001063	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Adenine nucleotide alpha hydrolases-like	8032265	3001593	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Argininosuccinate synthetase, C-terminal domain	8032266	3001063	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Adenine nucleotide alpha hydrolases-like	8032265	3001593	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Adenine nucleotide alpha hydrolases-like	8032265	3001593	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Argininosuccinate synthetase, C-terminal domain	8032266	3001063	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)
C	Arginosuc_synth_C	e1j1zC1	A: a+b complex topology	X: Argininosuccinate synthetase-C (From Topology)	H: Argininosuccinate synthetase-C (From Topology)	T: Argininosuccinate synthetase-C	F: Arginosuc_synth_C	ECOD (1.6)
C	Arginosuc_synth_N	e1j1zC2	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: Arginosuc_synth_N	ECOD (1.6)
D	Arginosuc_synth_C	e1j1zD1	A: a+b complex topology	X: Argininosuccinate synthetase-C (From Topology)	H: Argininosuccinate synthetase-C (From Topology)	T: Argininosuccinate synthetase-C	F: Arginosuc_synth_C	ECOD (1.6)
D	Arginosuc_synth_N	e1j1zD2	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: Arginosuc_synth_N	ECOD (1.6)
A	Arginosuc_synth_C	e1j1zA1	A: a+b complex topology	X: Argininosuccinate synthetase-C (From Topology)	H: Argininosuccinate synthetase-C (From Topology)	T: Argininosuccinate synthetase-C	F: Arginosuc_synth_C	ECOD (1.6)
A	Arginosuc_synth_N	e1j1zA2	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: Arginosuc_synth_N	ECOD (1.6)
B	Arginosuc_synth_C	e1j1zB1	A: a+b complex topology	X: Argininosuccinate synthetase-C (From Topology)	H: Argininosuccinate synthetase-C (From Topology)	T: Argininosuccinate synthetase-C	F: Arginosuc_synth_C	ECOD (1.6)
B	Arginosuc_synth_N	e1j1zB2	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: Arginosuc_synth_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
C	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)
C	3.90.1260.10	Alpha Beta	Alpha-Beta Complex	Argininosuccinate synthetase, chain A, domain 2	Argininosuccinate synthetase, chain A, domain 2	CATH (4.3.0)
D	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)
D	3.90.1260.10	Alpha Beta	Alpha-Beta Complex	Argininosuccinate synthetase, chain A, domain 2	Argininosuccinate synthetase, chain A, domain 2	CATH (4.3.0)
A	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)
A	3.90.1260.10	Alpha Beta	Alpha-Beta Complex	Argininosuccinate synthetase, chain A, domain 2	Argininosuccinate synthetase, chain A, domain 2	CATH (4.3.0)
B	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)
B	3.90.1260.10	Alpha Beta	Alpha-Beta Complex	Argininosuccinate synthetase, chain A, domain 2	Argininosuccinate synthetase, chain A, domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF20979	Arginosuccinate synthase C-terminal domain (Arginosuc_syn_C)	Arginosuccinate synthase C-terminal domain	This entry represents the C-terminal domain of the Arginosuccinate synthase enzyme.	Domain
A, B, C, D	PF00764	Arginosuccinate synthase N-terminal HUP domain (Arginosuc_synth)	Arginosuccinate synthase N-terminal HUP domain	This entry represents the N-terminal domain of the Arginosuccinate synthase enzyme. This domain is part of the HUP superfamily.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Argininosuccinate Synthetase	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding argininosuccinate synthase activity catalytic activity ligase activity, forming carbon-nitrogen bonds ligase 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	cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR018223	Argininosuccinate synthase, conserved site	Conserved Site
A, B, C, D	IPR048268	Arginosuccinate synthase C-terminal domain	Domain
A, B, C, D	IPR001518	Argininosuccinate synthase	Family
A, B, C, D	IPR023434	Argininosuccinate synthase, type 1 subfamily	Family
A, B, C, D	IPR048267	Arginosuccinate synthase-like, N-terminal domain	Domain
A, B, C, D	IPR024074	Argininosuccinate synthetase, catalytic/multimerisation domain body	Homologous Superfamily
A, B, C, D	IPR014729	Rossmann-like alpha/beta/alpha sandwich fold	Homologous Superfamily

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.