2GVD

Complex Of Gs- With The Catalytic Domains Of Mammalian Adenylyl Cyclase: Complex With TNP-ATP and Mn

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0009190	biological_process	cyclic nucleotide biosynthetic process
A	0016849	molecular_function	phosphorus-oxygen lyase activity
A	0035556	biological_process	intracellular signal transduction
B	0009190	biological_process	cyclic nucleotide biosynthetic process
B	0016849	molecular_function	phosphorus-oxygen lyase activity
B	0035556	biological_process	intracellular signal transduction
C	0003924	molecular_function	GTPase activity
C	0005159	molecular_function	insulin-like growth factor receptor binding
C	0005525	molecular_function	GTP binding
C	0005737	cellular_component	cytoplasm
C	0005834	cellular_component	heterotrimeric G-protein complex
C	0005886	cellular_component	plasma membrane
C	0007165	biological_process	signal transduction
C	0007186	biological_process	G protein-coupled receptor signaling pathway
C	0007189	biological_process	adenylate cyclase-activating G protein-coupled receptor signaling pathway
C	0007191	biological_process	adenylate cyclase-activating dopamine receptor signaling pathway
C	0007606	biological_process	sensory perception of chemical stimulus
C	0010856	molecular_function	adenylate cyclase activator activity
C	0019001	molecular_function	guanyl nucleotide binding
C	0031683	molecular_function	G-protein beta/gamma-subunit complex binding
C	0031698	molecular_function	beta-2 adrenergic receptor binding
C	0031748	molecular_function	D1 dopamine receptor binding
C	0031852	molecular_function	mu-type opioid receptor binding
C	0035255	molecular_function	ionotropic glutamate receptor binding
C	0046872	molecular_function	metal ion binding
C	0051430	molecular_function	corticotropin-releasing hormone receptor 1 binding
C	0071880	biological_process	adenylate cyclase-activating adrenergic receptor signaling pathway

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN C 396

Chain	Residue
C	SER54
C	THR204
C	GSP395

---

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL C 397

Chain	Residue
C	ALA48
C	ALA249
C	ARG265

---

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MN A 581

Chain	Residue
A	ASP396
A	ASP440

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN A 582

Chain	Residue
A	ILE397
A	ASP440
A	128584
A	ASP396

---

site_id	AC5
Number of Residues	21
Details	BINDING SITE FOR RESIDUE GSP C 395

Chain	Residue
C	GLU50
C	SER51
C	GLY52
C	LYS53
C	SER54
C	THR55
C	ASP173
C	LEU198
C	ARG199
C	CYS200
C	ARG201
C	THR204
C	GLY226
C	ASN292
C	LYS293
C	ASP295
C	LEU296
C	CYS365
C	ALA366
C	VAL367
C	MN396

---

site_id	AC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE FKP A 583

Chain	Residue
A	CYS441
A	TYR443
A	ASP505
A	VAL506
A	TRP507
A	SER508
A	VAL511
A	THR512
A	ASN515
B	PHE895
B	LYS896
B	TYR899
B	SER942

---

site_id	AC7
Number of Residues	18
Details	BINDING SITE FOR RESIDUE 128 A 584

Chain	Residue
A	HOH68
A	ILE397
A	GLY399
A	PHE400
A	ALA409
A	LEU412
A	VAL413
A	LEU416
A	GLY439
A	ASP440
A	ARG484
A	MN582
B	PHE889
B	TRP1020
B	ASN1022
B	ASN1025
B	SER1028
B	LYS1065

---

Functional Information from PROSITE/UniProt

site_id	PS00452
Number of Residues	24
Details	GUANYLATE_CYCLASE_1 Guanylate cyclase signature. GVI.GaqkpqYdIWGNTVNvasrmD

Chain	Residue	Details
B	GLY1008-ASP1031
A	GLY495-GLU518

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	5
Details	BINDING: BINDING => ECO:0000305|PubMed:10427002, ECO:0000305|PubMed:11087399, ECO:0000305|PubMed:15591060, ECO:0000305|PubMed:16766715, ECO:0000305|PubMed:19243146, ECO:0000305|PubMed:9395396, ECO:0000305|PubMed:9417641

Chain	Residue	Details
C	GLY47
C	LEU197
C	ASP223
C	ASN292
C	ALA366

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:10427002, ECO:0000269|PubMed:11087399, ECO:0000269|PubMed:15591060, ECO:0000269|PubMed:19243146, ECO:0000269|PubMed:9395396, ECO:0000269|PubMed:9417641, ECO:0000305|PubMed:16766715

Chain	Residue	Details
C	SER54
C	THR204

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P63092

Chain	Residue	Details
C	SER352

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	LIPID: N-palmitoyl glycine => ECO:0000269|PubMed:12574119

Chain	Residue	Details
C	GLY2

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	LIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:12574119

Chain	Residue	Details
C	CYS3

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P63092

Chain	Residue	Details
C	LYS300

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1ab8

Chain	Residue	Details
B	ARG1029

---

site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1ab8

Chain	Residue	Details
A	HIS516

---

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1ab8

Chain	Residue	Details
C	THR204
C	ARG201
C	GLU50
C	GLN227

---

site_id	CSA4
Number of Residues	1
Details	Annotated By Reference To The Literature 1ab8

Chain	Residue	Details
C	GLN227

---

site_id	MCSA1
Number of Residues	2
Details	M-CSA 58

Chain	Residue	Details
B	ARG1029	electrostatic stabiliser
B	LYS1065	electrostatic stabiliser
A	ASP440	metal ligand

---