5O5K

X-ray structure of a bacterial adenylyl cyclase soluble domain

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	SCOP2B Superfamily	Nucleotide cyclase/DNA polymerase palm domain-like	8079317	3001272	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Nucleotide cyclase/DNA polymerase palm domain-like	8079317	3001272	SCOP2B (2022-06-29)
C [auth D]	SCOP2B Superfamily	Nucleotide cyclase/DNA polymerase palm domain-like	8079317	3001272	SCOP2B (2022-06-29)
D [auth C]	SCOP2B Superfamily	Nucleotide cyclase/DNA polymerase palm domain-like	8079317	3001272	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Nucleotide cyclase/DNA polymerase palm domain-like	8079317	3001272	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Nucleotide cyclase/DNA polymerase palm domain-like	8079317	3001272	SCOP2B (2022-06-29)
G [auth I]	SCOP2B Superfamily	Nucleotide cyclase/DNA polymerase palm domain-like	8079317	3001272	SCOP2B (2022-06-29)
H [auth J]	SCOP2B Superfamily	Nucleotide cyclase/DNA polymerase palm domain-like	8079317	3001272	SCOP2B (2022-06-29)
I [auth H]	SCOP2B Superfamily	Nucleotide cyclase/DNA polymerase palm domain-like	8079317	3001272	SCOP2B (2022-06-29)
J [auth G]	SCOP2B Superfamily	Nucleotide cyclase/DNA polymerase palm domain-like	8079317	3001272	SCOP2B (2022-06-29)
K	SCOP2B Superfamily	Nucleotide cyclase/DNA polymerase palm domain-like	8079317	3001272	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	Guanylate_cyc	e5o5kA1	A: a+b two layers	X: Alpha-beta plaits	H: Adenylyl and guanylyl cyclase catalytic domain-like	T: Adenylyl and guanylyl cyclase catalytic domain-like	F: Guanylate_cyc	ECOD (1.6)
B	Guanylate_cyc	e5o5kB1	A: a+b two layers	X: Alpha-beta plaits	H: Adenylyl and guanylyl cyclase catalytic domain-like	T: Adenylyl and guanylyl cyclase catalytic domain-like	F: Guanylate_cyc	ECOD (1.6)
C [auth D]	Guanylate_cyc	e5o5kD1	A: a+b two layers	X: Alpha-beta plaits	H: Adenylyl and guanylyl cyclase catalytic domain-like	T: Adenylyl and guanylyl cyclase catalytic domain-like	F: Guanylate_cyc	ECOD (1.6)
D [auth C]	Guanylate_cyc	e5o5kC1	A: a+b two layers	X: Alpha-beta plaits	H: Adenylyl and guanylyl cyclase catalytic domain-like	T: Adenylyl and guanylyl cyclase catalytic domain-like	F: Guanylate_cyc	ECOD (1.6)
E	Guanylate_cyc	e5o5kE1	A: a+b two layers	X: Alpha-beta plaits	H: Adenylyl and guanylyl cyclase catalytic domain-like	T: Adenylyl and guanylyl cyclase catalytic domain-like	F: Guanylate_cyc	ECOD (1.6)
F	Guanylate_cyc	e5o5kF1	A: a+b two layers	X: Alpha-beta plaits	H: Adenylyl and guanylyl cyclase catalytic domain-like	T: Adenylyl and guanylyl cyclase catalytic domain-like	F: Guanylate_cyc	ECOD (1.6)
G [auth I]	Guanylate_cyc	e5o5kI1	A: a+b two layers	X: Alpha-beta plaits	H: Adenylyl and guanylyl cyclase catalytic domain-like	T: Adenylyl and guanylyl cyclase catalytic domain-like	F: Guanylate_cyc	ECOD (1.6)
H [auth J]	Guanylate_cyc	e5o5kJ1	A: a+b two layers	X: Alpha-beta plaits	H: Adenylyl and guanylyl cyclase catalytic domain-like	T: Adenylyl and guanylyl cyclase catalytic domain-like	F: Guanylate_cyc	ECOD (1.6)
I [auth H]	Guanylate_cyc	e5o5kH1	A: a+b two layers	X: Alpha-beta plaits	H: Adenylyl and guanylyl cyclase catalytic domain-like	T: Adenylyl and guanylyl cyclase catalytic domain-like	F: Guanylate_cyc	ECOD (1.6)
J [auth G]	Guanylate_cyc	e5o5kG1	A: a+b two layers	X: Alpha-beta plaits	H: Adenylyl and guanylyl cyclase catalytic domain-like	T: Adenylyl and guanylyl cyclase catalytic domain-like	F: Guanylate_cyc	ECOD (1.6)
K	Guanylate_cyc	e5o5kK1	A: a+b two layers	X: Alpha-beta plaits	H: Adenylyl and guanylyl cyclase catalytic domain-like	T: Adenylyl and guanylyl cyclase catalytic domain-like	F: Guanylate_cyc	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.70.1230	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Nucleotide cyclase, GGDEF domain	CATH (4.3.0)
B	3.30.70.1230	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Nucleotide cyclase, GGDEF domain	CATH (4.3.0)
C [auth D]	3.30.70.1230	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Nucleotide cyclase, GGDEF domain	CATH (4.3.0)
D [auth C]	3.30.70.1230	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Nucleotide cyclase, GGDEF domain	CATH (4.3.0)
E	3.30.70.1230	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Nucleotide cyclase, GGDEF domain	CATH (4.3.0)
F	3.30.70.1230	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Nucleotide cyclase, GGDEF domain	CATH (4.3.0)
G [auth I]	3.30.70.1230	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Nucleotide cyclase, GGDEF domain	CATH (4.3.0)
H [auth J]	3.30.70.1230	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Nucleotide cyclase, GGDEF domain	CATH (4.3.0)
I [auth H]	3.30.70.1230	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Nucleotide cyclase, GGDEF domain	CATH (4.3.0)
J [auth G]	3.30.70.1230	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Nucleotide cyclase, GGDEF domain	CATH (4.3.0)
K	3.30.70.1230	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Nucleotide cyclase, GGDEF domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C [auth D], D [auth C], E, A, B, C [auth D], D [auth C], E, F, G [auth I], H [auth J], I [auth H], J [auth G], K	PF00211	Adenylate and Guanylate cyclase catalytic domain (Guanylate_cyc)	Adenylate and Guanylate cyclase catalytic domain	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C [auth D], D [auth C], E, A, B, C [auth D], D [auth C], E, F, G [auth I], H [auth J], I [auth H], J [auth G], K	Adenylate cyclase	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 phosphorus-oxygen lyase activity cyclase activity lyase activity adenylate cyclase activity catalytic activity cation binding metal ion binding	cellular response to stimulus regulation of biological process regulation of cellular process response to stimulus signaling biological regulation adenylate cyclase-activating G protein-coupled receptor signaling pathway cell communication adenylate cyclase-modulating G protein-coupled receptor signaling pathway G protein-coupled receptor signaling pathway cellular process signal transduction intracellular signal transduction ribose phosphate metabolic process cellular response to stimulus regulation of biological process regulation of cellular process response to stimulus signaling biological regulation adenylate cyclase-activating G protein-coupled receptor signaling pathway cell communication adenylate cyclase-modulating G protein-coupled receptor signaling pathway G protein-coupled receptor signaling pathway cellular process signal transduction intracellular signal transduction ribose phosphate metabolic process nucleotide biosynthetic process carbohydrate derivative metabolic process purine ribonucleotide biosynthetic process cAMP biosynthetic process cyclic nucleotide metabolic process nucleobase-containing compound metabolic process ribonucleotide biosynthetic process purine nucleotide metabolic process ribonucleotide metabolic process nucleobase-containing small molecule metabolic process purine-containing compound biosynthetic process cyclic nucleotide biosynthetic process phosphate-containing compound metabolic process small molecule metabolic process phosphorus metabolic process ribose phosphate biosynthetic process nucleoside phosphate metabolic process carbohydrate derivative biosynthetic process cAMP metabolic process cyclic purine nucleotide metabolic process cellular metabolic process primary metabolic process nucleotide metabolic process nucleobase-containing compound biosynthetic process purine-containing compound metabolic process biosynthetic process organophosphate metabolic process organophosphate biosynthetic process nucleoside phosphate biosynthetic process metabolic process purine ribonucleotide metabolic process purine nucleotide biosynthetic process	membrane cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C [auth D], D [auth C], E, A, B, C [auth D], D [auth C], E, F, G [auth I], H [auth J], I [auth H], J [auth G], K	IPR018297	Adenylyl cyclase class-4/guanylyl cyclase, conserved site	Conserved Site
A, B, C [auth D], D [auth C], E, A, B, C [auth D], D [auth C], E, F, G [auth I], H [auth J], I [auth H], J [auth G], K	IPR001054	Adenylyl cyclase class-3/4/guanylyl cyclase	Domain
A, B, C [auth D], D [auth C], E, A, B, C [auth D], D [auth C], E, F, G [auth I], H [auth J], I [auth H], J [auth G], K	IPR048432	Adenylate cyclase, MASE7	Domain
A, B, C [auth D], D [auth C], E, A, B, C [auth D], D [auth C], E, F, G [auth I], H [auth J], I [auth H], J [auth G], K	IPR029787	Nucleotide cyclase	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.