5O5L

X-ray structure of a bacterial adenylyl cyclase soluble domain, solved at cryogenic temperature

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	Adenylyl and guanylyl cyclase catalytic domain	8079316	4001316	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Nucleotide cyclase/DNA polymerase palm domain-like	8079317	3001272	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Nucleotide cyclase/DNA polymerase palm domain-like	8079317	3001272	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Nucleotide cyclase/DNA polymerase palm domain-like	8079317	3001272	SCOP2B (2022-06-29)
D	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	SCOP2B Superfamily	Nucleotide cyclase/DNA polymerase palm domain-like	8079317	3001272	SCOP2B (2022-06-29)
H	SCOP2B Superfamily	Nucleotide cyclase/DNA polymerase palm domain-like	8079317	3001272	SCOP2B (2022-06-29)
I	SCOP2B Superfamily	Nucleotide cyclase/DNA polymerase palm domain-like	8079317	3001272	SCOP2B (2022-06-29)
J	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	PF00211	e5o5lA1	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: PF00211	ECOD (1.6)
B	PF00211	e5o5lB1	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: PF00211	ECOD (1.6)
C	PF00211	e5o5lC1	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: PF00211	ECOD (1.6)
D	PF00211	e5o5lD1	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: PF00211	ECOD (1.6)
E	PF00211	e5o5lE1	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: PF00211	ECOD (1.6)
F	PF00211	e5o5lF1	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: PF00211	ECOD (1.6)
G	PF00211	e5o5lG1	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: PF00211	ECOD (1.6)
H	PF00211	e5o5lH1	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: PF00211	ECOD (1.6)
I	PF00211	e5o5lI1	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: PF00211	ECOD (1.6)
J	PF00211	e5o5lJ1	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: PF00211	ECOD (1.6)
K	PF00211	e5o5lK1	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: PF00211	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	3.30.70.1230	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Nucleotide cyclase, GGDEF domain	CATH (4.3.0)
D	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	3.30.70.1230	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Nucleotide cyclase, GGDEF domain	CATH (4.3.0)
H	3.30.70.1230	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Nucleotide cyclase, GGDEF domain	CATH (4.3.0)
I	3.30.70.1230	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Nucleotide cyclase, GGDEF domain	CATH (4.3.0)
J	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, D, E A, B, C, D, E, F, G, H, I, J, K	PF20967	MASE7 (MASE7)	MASE7	This entry represents a predicted integral membrane sensor domain (MASE7) [1], which is found in association with GGDEF domain (Pfam:PF00990), histidine sensor kinases and adenylate cyclase output domain (Pfam:PF00211).	Domain
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, 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, D, E A, B, C, D, E, F, G, H, I, J, K	Adenylate cyclase	phosphorus-oxygen lyase activity cyclase activity lyase activity adenylate cyclase activity catalytic activity	cellular response to stimulus regulation of biological process regulation of cellular process response to stimulus signaling biological regulation cellular process signal transduction intracellular signal transduction cell communication nucleotide biosynthetic process cyclic nucleotide metabolic process nucleobase-containing compound metabolic process organic substance metabolic process cellular response to stimulus regulation of biological process regulation of cellular process response to stimulus signaling biological regulation cellular process signal transduction intracellular signal transduction cell communication nucleotide biosynthetic process cyclic nucleotide metabolic process nucleobase-containing compound metabolic process organic substance metabolic process nucleobase-containing small molecule metabolic process cyclic nucleotide biosynthetic process organic substance biosynthetic process phosphate-containing compound metabolic process small molecule metabolic process phosphorus metabolic process nucleoside phosphate metabolic process cellular metabolic process primary metabolic process nucleobase-containing compound biosynthetic process nucleotide metabolic process organic cyclic compound metabolic process biosynthetic process organophosphate metabolic process organophosphate biosynthetic process organic cyclic compound biosynthetic process nucleoside phosphate biosynthetic process metabolic process	membrane cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K	IPR018297	Adenylyl cyclase class-4/guanylyl cyclase, conserved site	Conserved Site
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K	IPR001054	Adenylyl cyclase class-3/4/guanylyl cyclase	Domain
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K	IPR048432	Adenylate cyclase, MASE7	Domain
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, 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 R01GM133198.