2DGB

Structure of Thermus thermophilus PurS in the P21 Form

External Resource: Annotation

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: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	PurS subunit of FGAM synthetase	8099903	4003257	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	PurS-like	8099904	3000512	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	PurS-like	8099904	3000512	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	PurS-like	8099904	3000512	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	PurS-like	8099904	3000512	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	PurS	e2dgbA1	A: a+b two layers	X: Alpha-beta plaits	H: PurS-like (From Topology)	T: PurS-like	F: PurS	ECOD (1.6)
B	PurS	e2dgbB1	A: a+b two layers	X: Alpha-beta plaits	H: PurS-like (From Topology)	T: PurS-like	F: PurS	ECOD (1.6)
C	PurS	e2dgbC1	A: a+b two layers	X: Alpha-beta plaits	H: PurS-like (From Topology)	T: PurS-like	F: PurS	ECOD (1.6)
D	PurS	e2dgbD1	A: a+b two layers	X: Alpha-beta plaits	H: PurS-like (From Topology)	T: PurS-like	F: PurS	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.1280.10	Alpha Beta	2-Layer Sandwich	Mth169	Chain: A ,	CATH (4.3.0)
B	3.30.1280.10	Alpha Beta	2-Layer Sandwich	Mth169	Chain: A ,	CATH (4.3.0)
C	3.30.1280.10	Alpha Beta	2-Layer Sandwich	Mth169	Chain: A ,	CATH (4.3.0)
D	3.30.1280.10	Alpha Beta	2-Layer Sandwich	Mth169	Chain: A ,	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF02700	Phosphoribosylformylglycinamidine (FGAM) synthase (PurS)	Phosphoribosylformylglycinamidine (FGAM) synthase	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	hypothetical protein PurS	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 carbon-nitrogen ligase activity, with glutamine as amido-N-donor phosphoribosylformylglycinamidine synthase activity catalytic activity ligase activity, forming carbon-nitrogen bonds ligase activity	ribose phosphate metabolic process IMP metabolic process purine ribonucleoside monophosphate biosynthetic process nucleotide biosynthetic process organonitrogen compound biosynthetic process carbohydrate derivative metabolic process purine ribonucleotide biosynthetic process nucleobase-containing compound metabolic process ribonucleotide biosynthetic process purine nucleoside monophosphate biosynthetic process purine ribonucleoside monophosphate metabolic process purine nucleotide metabolic process organic substance metabolic process ribonucleotide metabolic process ribonucleoside monophosphate metabolic process ribose phosphate metabolic process IMP metabolic process purine ribonucleoside monophosphate biosynthetic process nucleotide biosynthetic process organonitrogen compound biosynthetic process carbohydrate derivative metabolic process purine ribonucleotide biosynthetic process nucleobase-containing compound metabolic process ribonucleotide biosynthetic process purine nucleoside monophosphate biosynthetic process purine ribonucleoside monophosphate metabolic process purine nucleotide metabolic process organic substance metabolic process ribonucleotide metabolic process ribonucleoside monophosphate metabolic process nucleobase-containing small molecule metabolic process purine-containing compound biosynthetic process purine nucleoside monophosphate metabolic process phosphate-containing compound metabolic process organic substance biosynthetic process small molecule metabolic process phosphorus metabolic process ribose phosphate biosynthetic process nucleoside monophosphate metabolic process nucleoside phosphate metabolic process carbohydrate derivative biosynthetic process organonitrogen compound metabolic process cellular metabolic process primary metabolic process nucleotide metabolic process nucleobase-containing compound biosynthetic process nucleoside monophosphate biosynthetic process purine-containing compound metabolic process organic cyclic compound metabolic process IMP biosynthetic process biosynthetic process organophosphate metabolic process organophosphate biosynthetic process organic cyclic compound biosynthetic process nucleoside phosphate biosynthetic process metabolic process cellular process 'de novo' IMP biosynthetic process purine ribonucleotide metabolic process ribonucleoside monophosphate biosynthetic process purine nucleotide biosynthetic process	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR036604	Phosphoribosylformylglycinamidine synthase subunit PurS-like superfamily	Homologous Superfamily
A, B, C, D	IPR003850	Phosphoribosylformylglycinamidine synthase subunit PurS	Family

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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.