4YB6

Adenosine triphosphate phosphoribosyltransferase from Campylobacter jejuni in complex with the inhibitors AMP and histidine

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)
E	d4yb6e1	Alpha and beta proteins (a/b)	Periplasmic binding protein-like II	Periplasmic binding protein-like II	automated matches	automated matches	(Campylobacter jejuni RM1221 ) [TaxId: 195099 ],	SCOPe (2.08)
E	d4yb6e2	Alpha and beta proteins (a+b)	Ferredoxin-like	GlnB-like	automated matches	automated matches	(Campylobacter jejuni RM1221 ) [TaxId: 195099 ],	SCOPe (2.08)
A	d4yb6a1	Alpha and beta proteins (a/b)	Periplasmic binding protein-like II	Periplasmic binding protein-like II	automated matches	automated matches	(Campylobacter jejuni RM1221 ) [TaxId: 195099 ],	SCOPe (2.08)
A	d4yb6a2	Alpha and beta proteins (a+b)	Ferredoxin-like	GlnB-like	automated matches	automated matches	(Campylobacter jejuni RM1221 ) [TaxId: 195099 ],	SCOPe (2.08)
B	d4yb6b1	Alpha and beta proteins (a/b)	Periplasmic binding protein-like II	Periplasmic binding protein-like II	automated matches	automated matches	(Campylobacter jejuni RM1221 ) [TaxId: 195099 ],	SCOPe (2.08)
B	d4yb6b2	Alpha and beta proteins (a+b)	Ferredoxin-like	GlnB-like	automated matches	automated matches	(Campylobacter jejuni RM1221 ) [TaxId: 195099 ],	SCOPe (2.08)
C	d4yb6c1	Alpha and beta proteins (a/b)	Periplasmic binding protein-like II	Periplasmic binding protein-like II	automated matches	automated matches	(Campylobacter jejuni RM1221 ) [TaxId: 195099 ],	SCOPe (2.08)
C	d4yb6c2	Alpha and beta proteins (a+b)	Ferredoxin-like	GlnB-like	automated matches	automated matches	(Campylobacter jejuni RM1221 ) [TaxId: 195099 ],	SCOPe (2.08)
D	d4yb6d1	Alpha and beta proteins (a/b)	Periplasmic binding protein-like II	Periplasmic binding protein-like II	automated matches	automated matches	(Campylobacter jejuni RM1221 ) [TaxId: 195099 ],	SCOPe (2.08)
D	d4yb6d2	Alpha and beta proteins (a+b)	Ferredoxin-like	GlnB-like	automated matches	automated matches	(Campylobacter jejuni RM1221 ) [TaxId: 195099 ],	SCOPe (2.08)
F	d4yb6f1	Alpha and beta proteins (a/b)	Periplasmic binding protein-like II	Periplasmic binding protein-like II	automated matches	automated matches	(Campylobacter jejuni RM1221 ) [TaxId: 195099 ],	SCOPe (2.08)
F	d4yb6f2	Alpha and beta proteins (a+b)	Ferredoxin-like	GlnB-like	automated matches	automated matches	(Campylobacter jejuni RM1221 ) [TaxId: 195099 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
E	SCOP2B Superfamily	Type 2 solute binding protein-like	8082641	3000083	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Type 2 solute binding protein-like	8082641	3000083	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Type 2 solute binding protein-like	8082641	3000083	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Type 2 solute binding protein-like	8082641	3000083	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Type 2 solute binding protein-like	8082641	3000083	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Type 2 solute binding protein-like	8082641	3000083	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)
E	HisG_C	e4yb6E3	A: a+b two layers	X: Alpha-beta plaits	H: GlnB-like (From Topology)	T: GlnB-like	F: HisG_C	ECOD (1.6)
E	HisG_N2	e4yb6E1	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: HisG_N2	ECOD (1.6)
E	HisG_N1	e4yb6E2	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: HisG_N1	ECOD (1.6)
A	HisG_C	e4yb6A3	A: a+b two layers	X: Alpha-beta plaits	H: GlnB-like (From Topology)	T: GlnB-like	F: HisG_C	ECOD (1.6)
A	HisG_N2	e4yb6A1	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: HisG_N2	ECOD (1.6)
A	HisG_N1	e4yb6A2	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: HisG_N1	ECOD (1.6)
B	HisG_C	e4yb6B2	A: a+b two layers	X: Alpha-beta plaits	H: GlnB-like (From Topology)	T: GlnB-like	F: HisG_C	ECOD (1.6)
B	HisG_N2	e4yb6B3	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: HisG_N2	ECOD (1.6)
B	HisG_N1	e4yb6B1	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: HisG_N1	ECOD (1.6)
C	HisG_C	e4yb6C1	A: a+b two layers	X: Alpha-beta plaits	H: GlnB-like (From Topology)	T: GlnB-like	F: HisG_C	ECOD (1.6)
C	HisG_N2	e4yb6C3	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: HisG_N2	ECOD (1.6)
C	HisG_N1	e4yb6C2	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: HisG_N1	ECOD (1.6)
D	HisG_C	e4yb6D2	A: a+b two layers	X: Alpha-beta plaits	H: GlnB-like (From Topology)	T: GlnB-like	F: HisG_C	ECOD (1.6)
D	HisG_N2	e4yb6D1	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: HisG_N2	ECOD (1.6)
D	HisG_N1	e4yb6D3	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: HisG_N1	ECOD (1.6)
F	HisG_C	e4yb6F3	A: a+b two layers	X: Alpha-beta plaits	H: GlnB-like (From Topology)	T: GlnB-like	F: HisG_C	ECOD (1.6)
F	HisG_N2	e4yb6F1	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: HisG_N2	ECOD (1.6)
F	HisG_N1	e4yb6F2	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: HisG_N1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
E	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
E	3.30.70.120	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits		CATH (4.3.0)
A	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
A	3.30.70.120	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits		CATH (4.3.0)
B	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
B	3.30.70.120	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits		CATH (4.3.0)
C	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
C	3.30.70.120	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits		CATH (4.3.0)
D	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
D	3.30.70.120	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits		CATH (4.3.0)
F	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
F	3.30.70.120	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits		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	PF01634	ATP phosphoribosyltransferase (HisG)	ATP phosphoribosyltransferase	-	Family
A, B, C, D, E A, B, C, D, E, F	PF08029	HisG, C-terminal domain (HisG_C)	HisG, C-terminal domain	-	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	ATP phosphoribosyltransferase	cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding anion binding cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding pentosyltransferase activity glycosyltransferase activity ATP phosphoribosyltransferase activity transferase activity catalytic activity	oxoacid metabolic process amino acid metabolic process organic acid biosynthetic process organic acid metabolic process imidazole-containing compound metabolic process alpha-amino acid metabolic process carboxylic acid biosynthetic process small molecule metabolic process aromatic amino acid family biosynthetic process aromatic amino acid metabolic process small molecule biosynthetic process L-histidine metabolic process carboxylic acid metabolic process primary metabolic process oxoacid metabolic process amino acid metabolic process organic acid biosynthetic process organic acid metabolic process imidazole-containing compound metabolic process alpha-amino acid metabolic process carboxylic acid biosynthetic process small molecule metabolic process aromatic amino acid family biosynthetic process aromatic amino acid metabolic process small molecule biosynthetic process L-histidine metabolic 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 L-histidine 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, E A, B, C, D, E, F	IPR015867	Nitrogen regulatory protein PII/ATP phosphoribosyltransferase, C-terminal	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR013820	ATP phosphoribosyltransferase, catalytic domain	Domain
A, B, C, D, E A, B, C, D, E, F	IPR011322	Nitrogen regulatory PII-like, alpha/beta	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR020621	ATP phosphoribosyltransferase HisG, long form	Family
A, B, C, D, E A, B, C, D, E, F	IPR018198	ATP phosphoribosyltransferase, conserved site	Conserved Site
A, B, C, D, E A, B, C, D, E, F	IPR013115	Histidine biosynthesis HisG, C-terminal	Domain
A, B, C, D, E A, B, C, D, E, F	IPR001348	ATP phosphoribosyltransferase HisG	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.