4CNZ

Structure of PII signaling protein GlnZ from Azospirillum brasilense in complex with adenosine diphosphate

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)
F	d4cnzf_	Alpha and beta proteins (a+b)	Ferredoxin-like	GlnB-like	Prokaryotic signal transducing protein	automated matches	(Azospirillum brasilense ) [TaxId: 192 ],	SCOPe (2.08)
A	d4cnza_	Alpha and beta proteins (a+b)	Ferredoxin-like	GlnB-like	Prokaryotic signal transducing protein	automated matches	(Azospirillum brasilense ) [TaxId: 192 ],	SCOPe (2.08)
B	d4cnzb_	Alpha and beta proteins (a+b)	Ferredoxin-like	GlnB-like	Prokaryotic signal transducing protein	automated matches	(Azospirillum brasilense ) [TaxId: 192 ],	SCOPe (2.08)
C	d4cnzc_	Alpha and beta proteins (a+b)	Ferredoxin-like	GlnB-like	Prokaryotic signal transducing protein	automated matches	(Azospirillum brasilense ) [TaxId: 192 ],	SCOPe (2.08)
D	d4cnzd_	Alpha and beta proteins (a+b)	Ferredoxin-like	GlnB-like	Prokaryotic signal transducing protein	automated matches	(Azospirillum brasilense ) [TaxId: 192 ],	SCOPe (2.08)
E	d4cnze_	Alpha and beta proteins (a+b)	Ferredoxin-like	GlnB-like	Prokaryotic signal transducing protein	automated matches	(Azospirillum brasilense ) [TaxId: 192 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
F	SCOP2B Superfamily	GlnB-like	8074417	3001165	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	GlnB-like	8074417	3001165	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	GlnB-like	8074417	3001165	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	GlnB-like	8074417	3001165	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	GlnB-like	8074417	3001165	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	GlnB-like	8074417	3001165	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)
F	P-II	e4cnzF1	A: a+b two layers	X: Alpha-beta plaits	H: GlnB-like (From Topology)	T: GlnB-like	F: P-II	ECOD (1.6)
A	P-II	e4cnzA1	A: a+b two layers	X: Alpha-beta plaits	H: GlnB-like (From Topology)	T: GlnB-like	F: P-II	ECOD (1.6)
B	P-II	e4cnzB1	A: a+b two layers	X: Alpha-beta plaits	H: GlnB-like (From Topology)	T: GlnB-like	F: P-II	ECOD (1.6)
C	P-II	e4cnzC1	A: a+b two layers	X: Alpha-beta plaits	H: GlnB-like (From Topology)	T: GlnB-like	F: P-II	ECOD (1.6)
D	P-II	e4cnzD1	A: a+b two layers	X: Alpha-beta plaits	H: GlnB-like (From Topology)	T: GlnB-like	F: P-II	ECOD (1.6)
E	P-II	e4cnzE1	A: a+b two layers	X: Alpha-beta plaits	H: GlnB-like (From Topology)	T: GlnB-like	F: P-II	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
F	3.30.70.120	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits		CATH (4.3.0)
A	3.30.70.120	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits		CATH (4.3.0)
B	3.30.70.120	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits		CATH (4.3.0)
C	3.30.70.120	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits		CATH (4.3.0)
D	3.30.70.120	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits		CATH (4.3.0)
E	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	PF00543	Nitrogen regulatory protein P-II (P-II)	Nitrogen regulatory protein P-II	P-II modulates the activity of glutamine synthetase. It is a tetrameric protein encoded by the glnB gene, a component of the adenylation cascade involved in the regulation of GS activity [1,2].	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	PII-LIKE PROTEIN PZ	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 enzyme regulator activity molecular function regulator activity cation binding metal ion binding	response to nutrient levels regulation of response to nutrient levels regulation of biological process response to stimulus homeostatic process nitrogen utilization biological regulation regulation of nitrogen utilization cellular homeostasis chemical homeostasis regulation of response to stimulus intracellular nitrogen homeostasis intracellular chemical homeostasis	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol

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	IPR011322	Nitrogen regulatory PII-like, alpha/beta	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR002187	Nitrogen regulatory protein PII	Family
A, B, C, D, E A, B, C, D, E, F	IPR002332	Nitrogen regulatory protein P-II, urydylation site	PTM
A, B, C, D, E A, B, C, D, E, F	IPR017918	Nitrogen regulatory protein PII, conserved site	Conserved Site

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.