6R4O

Structure of a truncated adenylyl cyclase bound to MANT-GTP, forskolin and an activated stimulatory Galphas protein

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0001701	biological_process	in utero embryonic development
A	0004016	molecular_function	adenylate cyclase activity
A	0005524	molecular_function	ATP binding
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0005929	cellular_component	cilium
A	0006091	biological_process	generation of precursor metabolites and energy
A	0006171	biological_process	cAMP biosynthetic process
A	0007189	biological_process	adenylate cyclase-activating G protein-coupled receptor signaling pathway
A	0008218	biological_process	bioluminescence
A	0009190	biological_process	cyclic nucleotide biosynthetic process
A	0016020	cellular_component	membrane
A	0016829	molecular_function	lyase activity
A	0016849	molecular_function	phosphorus-oxygen lyase activity
A	0035556	biological_process	intracellular signal transduction
A	0036064	cellular_component	ciliary basal body
A	0046872	molecular_function	metal ion binding
A	0071880	biological_process	adenylate cyclase-activating adrenergic receptor signaling pathway
B	0003924	molecular_function	GTPase activity
B	0005525	molecular_function	GTP binding
B	0007165	biological_process	signal transduction
B	0007186	biological_process	G protein-coupled receptor signaling pathway
B	0019001	molecular_function	guanyl nucleotide binding
B	0031683	molecular_function	G-protein beta/gamma-subunit complex binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	binding site for residue ONM A 2000

Chain	Residue
A	ASP399
A	GLY442
A	ASP443
A	MET1116
A	TRP1188
A	GLY1189
A	ASP1190
A	ASN1193
A	MN2002
A	MN2003
A	ILE400
A	VAL401
A	GLY402
A	PHE403
A	THR404
A	SER407
A	LEU415
A	LEU441

---

site_id	AC2
Number of Residues	5
Details	binding site for residue FOK A 2001

Chain	Residue
A	SER511
A	ASN515
A	ASN518
A	ILE1111
A	ALA1113

---

site_id	AC3
Number of Residues	3
Details	binding site for residue MN A 2002

Chain	Residue
A	ASP399
A	ASP443
A	ONM2000

---

site_id	AC4
Number of Residues	4
Details	binding site for residue MN A 2003

Chain	Residue
A	ASP399
A	ILE400
A	VAL401
A	ONM2000

---

site_id	AC5
Number of Residues	22
Details	binding site for residue GSP B 501

Chain	Residue
B	ALA48
B	GLY49
B	GLU50
B	SER51
B	GLY52
B	LYS53
B	SER54
B	THR55
B	LEU198
B	ARG199
B	CYS200
B	ARG201
B	VAL202
B	THR204
B	VAL224
B	GLY225
B	ASN292
B	LYS293
B	LEU296
B	CYS365
B	ALA366
B	MG502

---

site_id	AC6
Number of Residues	4
Details	binding site for residue MG B 502

Chain	Residue
B	SER54
B	THR204
B	ASP223
B	GSP501

---

Functional Information from PROSITE/UniProt

site_id	PS00452
Number of Residues	24
Details	GUANYLATE_CYCLASE_1 Guanylate cyclase signature. GIL.GmrrfkFdVWSNDVNlanlmE

Chain	Residue	Details
A	GLY498-GLU521
A	GLY1176-ASP1199

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI3
Number of Residues	13
Details	Region: {"description":"G1 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	Region: {"description":"G2 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	9
Details	Region: {"description":"G3 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	7
Details	Region: {"description":"G4 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	5
Details	Region: {"description":"G5 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	23
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10427002","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"11087399","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15591060","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16766715","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19243146","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9395396","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9417641","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10427002","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11087399","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15591060","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19243146","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9395396","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9417641","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16766715","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P63092","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P63092","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---