6OY9

Structure of the Rhodopsin-Transducin Complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000035	molecular_function	acyl binding
A	0001664	molecular_function	G protein-coupled receptor binding
A	0001750	cellular_component	photoreceptor outer segment
A	0001917	cellular_component	photoreceptor inner segment
A	0003924	molecular_function	GTPase activity
A	0005515	molecular_function	protein binding
A	0005525	molecular_function	GTP binding
A	0005737	cellular_component	cytoplasm
A	0005834	cellular_component	heterotrimeric G-protein complex
A	0007165	biological_process	signal transduction
A	0007186	biological_process	G protein-coupled receptor signaling pathway
A	0007188	biological_process	adenylate cyclase-modulating G protein-coupled receptor signaling pathway
A	0007601	biological_process	visual perception
A	0007602	biological_process	phototransduction
A	0007603	biological_process	phototransduction, visible light
A	0009416	biological_process	response to light stimulus
A	0016020	cellular_component	membrane
A	0019001	molecular_function	guanyl nucleotide binding
A	0019003	molecular_function	GDP binding
A	0019901	molecular_function	protein kinase binding
A	0031683	molecular_function	G-protein beta/gamma-subunit complex binding
A	0042622	cellular_component	photoreceptor outer segment membrane
A	0042995	cellular_component	cell projection
A	0046872	molecular_function	metal ion binding
A	0050908	biological_process	detection of light stimulus involved in visual perception
A	0051344	biological_process	negative regulation of cyclic-nucleotide phosphodiesterase activity
A	0097381	cellular_component	photoreceptor disc membrane
A	0097648	cellular_component	G protein-coupled receptor complex
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005834	cellular_component	heterotrimeric G-protein complex
B	0007165	biological_process	signal transduction
B	0007186	biological_process	G protein-coupled receptor signaling pathway
B	0007191	biological_process	adenylate cyclase-activating dopamine receptor signaling pathway
B	0016020	cellular_component	membrane
B	0030159	molecular_function	signaling receptor complex adaptor activity
B	0071380	biological_process	cellular response to prostaglandin E stimulus
B	0071870	biological_process	cellular response to catecholamine stimulus
B	0097381	cellular_component	photoreceptor disc membrane
G	0005834	cellular_component	heterotrimeric G-protein complex
G	0005886	cellular_component	plasma membrane
G	0007165	biological_process	signal transduction
G	0007186	biological_process	G protein-coupled receptor signaling pathway
G	0031681	molecular_function	G-protein beta-subunit binding
G	0097381	cellular_component	photoreceptor disc membrane
R	0000139	cellular_component	Golgi membrane
R	0000226	biological_process	microtubule cytoskeleton organization
R	0001750	cellular_component	photoreceptor outer segment
R	0001917	cellular_component	photoreceptor inner segment
R	0001965	molecular_function	G-protein alpha-subunit binding
R	0002046	molecular_function	opsin binding
R	0004930	molecular_function	G protein-coupled receptor activity
R	0005085	molecular_function	guanyl-nucleotide exchange factor activity
R	0005502	molecular_function	11-cis retinal binding
R	0005515	molecular_function	protein binding
R	0005794	cellular_component	Golgi apparatus
R	0005886	cellular_component	plasma membrane
R	0005911	cellular_component	cell-cell junction
R	0007186	biological_process	G protein-coupled receptor signaling pathway
R	0007601	biological_process	visual perception
R	0007602	biological_process	phototransduction
R	0007603	biological_process	phototransduction, visible light
R	0008020	molecular_function	G protein-coupled photoreceptor activity
R	0008270	molecular_function	zinc ion binding
R	0009416	biological_process	response to light stimulus
R	0009583	biological_process	detection of light stimulus
R	0009642	biological_process	response to light intensity
R	0009881	molecular_function	photoreceptor activity
R	0010467	biological_process	gene expression
R	0016020	cellular_component	membrane
R	0016038	biological_process	absorption of visible light
R	0016056	biological_process	rhodopsin mediated signaling pathway
R	0016062	biological_process	obsolete adaptation of rhodopsin mediated signaling
R	0019867	cellular_component	outer membrane
R	0042622	cellular_component	photoreceptor outer segment membrane
R	0042802	molecular_function	identical protein binding
R	0042995	cellular_component	cell projection
R	0043052	biological_process	thermotaxis
R	0045494	biological_process	photoreceptor cell maintenance
R	0046872	molecular_function	metal ion binding
R	0050953	biological_process	sensory perception of light stimulus
R	0050960	biological_process	detection of temperature stimulus involved in thermoception
R	0060041	biological_process	retina development in camera-type eye
R	0060342	cellular_component	photoreceptor inner segment membrane
R	0071482	biological_process	cellular response to light stimulus
R	0071800	biological_process	podosome assembly
R	0097225	cellular_component	sperm midpiece
R	0097381	cellular_component	photoreceptor disc membrane
R	0097648	cellular_component	G protein-coupled receptor complex
R	0120200	cellular_component	rod photoreceptor outer segment
R	1904389	biological_process	rod bipolar cell differentiation
R	1990763	molecular_function	arrestin family protein binding
R	1990913	cellular_component	sperm head plasma membrane

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	binding site for residue RET R 401

Chain	Residue
R	ALA117
R	THR118
R	GLU122
R	MET207
R	TRP265
R	TYR268
R	ALA269
R	LYS296

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Functional Information from PROSITE/UniProt

site_id	PS00678
Number of Residues	15
Details	WD_REPEATS_1 Trp-Asp (WD) repeats signature. LLSAsqDgKLIIWDS

Chain	Residue	Details
B	LEU70-SER84
B	ILE157-ILE171
B	LEU285-ALA299

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site_id	PS00237
Number of Residues	17
Details	G_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. IALwSLVVLAIERYVvV

Chain	Residue	Details
R	ILE123-VAL139

---

site_id	PS00238
Number of Residues	17
Details	OPSIN Visual pigments (opsins) retinal binding site. IPaFfAKTSAvyNPviY

Chain	Residue	Details
R	ILE290-TYR306

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	87
Details	TOPO_DOM: Extracellular => ECO:0000269|PubMed:10926528, ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:11972040, ECO:0000269|PubMed:12044163, ECO:0000269|PubMed:15327956, ECO:0000269|PubMed:15491621, ECO:0000269|PubMed:16586416, ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:17060607, ECO:0000269|PubMed:17449675, ECO:0000269|PubMed:17825322, ECO:0000269|PubMed:18563085, ECO:0000269|PubMed:18645239, ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:21389983, ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23579341, ECO:0000269|PubMed:25205354, ECO:0000269|PubMed:26526852, ECO:0000269|PubMed:27458239

Chain	Residue	Details
R	MET1-GLN36
R	THR97-CYS110
R	GLY174-SER202
R	ILE275-ILE286

---

site_id	SWS_FT_FI2
Number of Residues	24
Details	TRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:10926528, ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:11972040, ECO:0000269|PubMed:12044163, ECO:0000269|PubMed:15327956, ECO:0000269|PubMed:15491621, ECO:0000269|PubMed:16586416, ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:17060607, ECO:0000269|PubMed:17449675, ECO:0000269|PubMed:17825322, ECO:0000269|PubMed:18563085, ECO:0000269|PubMed:18645239, ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:21389983, ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23579341, ECO:0000269|PubMed:25205354, ECO:0000269|PubMed:26526852, ECO:0000269|PubMed:27458239

Chain	Residue	Details
R	PHE37-VAL61
A	THR177

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site_id	SWS_FT_FI3
Number of Residues	95
Details	TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:10926528, ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:11972040, ECO:0000269|PubMed:12044163, ECO:0000269|PubMed:15327956, ECO:0000269|PubMed:15491621, ECO:0000269|PubMed:16586416, ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:17060607, ECO:0000269|PubMed:17449675, ECO:0000269|PubMed:17825322, ECO:0000269|PubMed:18563085, ECO:0000269|PubMed:18645239, ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:21389983, ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23579341, ECO:0000269|PubMed:25205354, ECO:0000269|PubMed:26526852, ECO:0000269|PubMed:27458239

Chain	Residue	Details
R	THR62-ASN73
R	GLU134-HIS152
R	GLN225-ARG252
R	MET309-ALA348

---

site_id	SWS_FT_FI4
Number of Residues	22
Details	TRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:10926528, ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:11972040, ECO:0000269|PubMed:12044163, ECO:0000269|PubMed:15327956, ECO:0000269|PubMed:15491621, ECO:0000269|PubMed:16586416, ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:17060607, ECO:0000269|PubMed:17449675, ECO:0000269|PubMed:17825322, ECO:0000269|PubMed:18563085, ECO:0000269|PubMed:18645239, ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:21389983, ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23579341, ECO:0000269|PubMed:25205354, ECO:0000269|PubMed:26526852, ECO:0000269|PubMed:27458239

Chain	Residue	Details
R	TYR74-TYR96

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site_id	SWS_FT_FI5
Number of Residues	22
Details	TRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:10926528, ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:11972040, ECO:0000269|PubMed:12044163, ECO:0000269|PubMed:15327956, ECO:0000269|PubMed:15491621, ECO:0000269|PubMed:16586416, ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:17060607, ECO:0000269|PubMed:17449675, ECO:0000269|PubMed:17825322, ECO:0000269|PubMed:18563085, ECO:0000269|PubMed:18645239, ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:21389983, ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23579341, ECO:0000269|PubMed:25205354, ECO:0000269|PubMed:26526852, ECO:0000269|PubMed:27458239

Chain	Residue	Details
R	ASN111-ILE133

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site_id	SWS_FT_FI6
Number of Residues	20
Details	TRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:10926528, ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:11972040, ECO:0000269|PubMed:12044163, ECO:0000269|PubMed:15327956, ECO:0000269|PubMed:15491621, ECO:0000269|PubMed:16586416, ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:17060607, ECO:0000269|PubMed:17449675, ECO:0000269|PubMed:17825322, ECO:0000269|PubMed:18563085, ECO:0000269|PubMed:18645239, ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:21389983, ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23579341, ECO:0000269|PubMed:25205354, ECO:0000269|PubMed:26526852, ECO:0000269|PubMed:27458239

Chain	Residue	Details
R	ALA153-VAL173

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site_id	SWS_FT_FI7
Number of Residues	21
Details	TRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:10926528, ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:11972040, ECO:0000269|PubMed:12044163, ECO:0000269|PubMed:15327956, ECO:0000269|PubMed:15491621, ECO:0000269|PubMed:16586416, ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:17060607, ECO:0000269|PubMed:17449675, ECO:0000269|PubMed:17825322, ECO:0000269|PubMed:18563085, ECO:0000269|PubMed:18645239, ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:21389983, ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23579341, ECO:0000269|PubMed:25205354, ECO:0000269|PubMed:26526852, ECO:0000269|PubMed:27458239

Chain	Residue	Details
R	PHE203-GLY224

---

site_id	SWS_FT_FI8
Number of Residues	21
Details	TRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:10926528, ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:11972040, ECO:0000269|PubMed:12044163, ECO:0000269|PubMed:15327956, ECO:0000269|PubMed:15491621, ECO:0000269|PubMed:16586416, ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:17060607, ECO:0000269|PubMed:17449675, ECO:0000269|PubMed:17825322, ECO:0000269|PubMed:18563085, ECO:0000269|PubMed:18645239, ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:21389983, ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23579341, ECO:0000269|PubMed:25205354, ECO:0000269|PubMed:26526852, ECO:0000269|PubMed:27458239

Chain	Residue	Details
R	MET253-TYR274

---

site_id	SWS_FT_FI9
Number of Residues	21
Details	TRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:10926528, ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:11972040, ECO:0000269|PubMed:12044163, ECO:0000269|PubMed:15327956, ECO:0000269|PubMed:15491621, ECO:0000269|PubMed:16586416, ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:17060607, ECO:0000269|PubMed:17449675, ECO:0000269|PubMed:17825322, ECO:0000269|PubMed:18563085, ECO:0000269|PubMed:18645239, ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:21389983, ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23579341, ECO:0000269|PubMed:25205354, ECO:0000269|PubMed:26526852, ECO:0000269|PubMed:27458239

Chain	Residue	Details
R	PHE287-MET308

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site_id	SWS_FT_FI10
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:10926528, ECO:0000269|PubMed:11425302, ECO:0007744|PDB:1F88, ECO:0007744|PDB:1HZX

Chain	Residue	Details
R	GLU201
R	GLN279

---

site_id	SWS_FT_FI11
Number of Residues	1
Details	SITE: Plays an important role in the conformation switch to the active conformation => ECO:0000269|PubMed:21389983, ECO:0000305|PubMed:22198838, ECO:0000305|PubMed:23579341, ECO:0000305|PubMed:27458239

Chain	Residue	Details
R	GLU113

---

site_id	SWS_FT_FI12
Number of Residues	1
Details	MOD_RES: N-acetylmethionine => ECO:0000305|PubMed:6759163

Chain	Residue	Details
R	MET1

---

site_id	SWS_FT_FI13
Number of Residues	1
Details	MOD_RES: N6-(retinylidene)lysine => ECO:0000269|PubMed:10926528, ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:11972040, ECO:0000269|PubMed:12044163, ECO:0000269|PubMed:15327956, ECO:0000269|PubMed:15491621, ECO:0000269|PubMed:16586416, ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:17449675, ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23303210, ECO:0000269|PubMed:27458239, ECO:0000269|PubMed:6870827, ECO:0000305|PubMed:6759163, ECO:0007744|PDB:1F88, ECO:0007744|PDB:1GZM, ECO:0007744|PDB:1HZX, ECO:0007744|PDB:1JFP, ECO:0007744|PDB:2HPY, ECO:0007744|PDB:3C9L, ECO:0007744|PDB:3OAX, ECO:0007744|PDB:3PQR, ECO:0007744|PDB:3PXO, ECO:0007744|PDB:5DYS

Chain	Residue	Details
R	LYS296

---

site_id	SWS_FT_FI14
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:15111114, ECO:0000269|PubMed:15351781

Chain	Residue	Details
R	SER334
R	SER338

---

site_id	SWS_FT_FI15
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0000269|PubMed:15111114, ECO:0000269|PubMed:15351781

Chain	Residue	Details
R	THR335
R	THR336
R	THR340
R	THR342

---

site_id	SWS_FT_FI16
Number of Residues	1
Details	MOD_RES: Phosphoserine; by RK and GRK7 => ECO:0000269|PubMed:1396673, ECO:0000269|PubMed:15111114, ECO:0000269|PubMed:15351781

Chain	Residue	Details
R	SER343

---

site_id	SWS_FT_FI17
Number of Residues	1
Details	LIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:11972040, ECO:0000269|PubMed:1512231, ECO:0000269|PubMed:15327956, ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:21389983, ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:26526852, ECO:0000269|PubMed:27458239, ECO:0000269|PubMed:3350146, ECO:0007744|PDB:1HZX, ECO:0007744|PDB:1L9H, ECO:0007744|PDB:2HPY, ECO:0007744|PDB:4X1H, ECO:0007744|PDB:5DYS

Chain	Residue	Details
R	CYS322

---

site_id	SWS_FT_FI18
Number of Residues	1
Details	LIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:11972040, ECO:0000269|PubMed:1512231, ECO:0000269|PubMed:15327956, ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:21389983, ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23579341, ECO:0000269|PubMed:25205354, ECO:0000269|PubMed:26526852, ECO:0000269|PubMed:27458239, ECO:0000269|PubMed:3350146, ECO:0007744|PDB:1HZX, ECO:0007744|PDB:1L9H, ECO:0007744|PDB:2HPY, ECO:0007744|PDB:4BEY, ECO:0007744|PDB:4PXF, ECO:0007744|PDB:4X1H, ECO:0007744|PDB:5DYS

Chain	Residue	Details
R	CYS323

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site_id	SWS_FT_FI19
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:15327956, ECO:0000269|PubMed:15491621, ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:26526852, ECO:0000269|PubMed:468821, ECO:0000269|PubMed:6759163, ECO:0007744|PDB:1F88, ECO:0007744|PDB:1GZM, ECO:0007744|PDB:1HZX, ECO:0007744|PDB:1U19, ECO:0007744|PDB:2G87, ECO:0007744|PDB:2HPY, ECO:0007744|PDB:2I35, ECO:0007744|PDB:2I36, ECO:0007744|PDB:2I37, ECO:0007744|PDB:2PED, ECO:0007744|PDB:3C9L, ECO:0007744|PDB:3CAP, ECO:0007744|PDB:3DQB, ECO:0007744|PDB:3OAX, ECO:0007744|PDB:3PQR, ECO:0007744|PDB:3PXO, ECO:0007744|PDB:4X1H

Chain	Residue	Details
R	ASN2

---

site_id	SWS_FT_FI20
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:11972040, ECO:0000269|PubMed:15327956, ECO:0000269|PubMed:15491621, ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:21389983, ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23579341, ECO:0000269|PubMed:25205354, ECO:0000269|PubMed:26526852, ECO:0000269|PubMed:468821, ECO:0000269|PubMed:6759163, ECO:0007744|PDB:1F88, ECO:0007744|PDB:1GZM, ECO:0007744|PDB:1HZX, ECO:0007744|PDB:1L9H, ECO:0007744|PDB:1U19, ECO:0007744|PDB:2G87, ECO:0007744|PDB:2HPY, ECO:0007744|PDB:2I35, ECO:0007744|PDB:2I36, ECO:0007744|PDB:2I37, ECO:0007744|PDB:2J4Y, ECO:0007744|PDB:2PED, ECO:0007744|PDB:2X72, ECO:0007744|PDB:3C9L, ECO:0007744|PDB:3C9M, ECO:0007744|PDB:3CAP, ECO:0007744|PDB:3DQB, ECO:0007744|PDB:3OAX, ECO:0007744|PDB:3PQR, ECO:0007744|PDB:3PXO, ECO:0007744|PDB:4A4M, ECO:0007744|PDB:4BEY, ECO:0007744|PDB:4BEZ, ECO:0007744|PDB:4J4Q, ECO:0007744|PDB:4PXF, ECO:0007744|PDB:4X1H, ECO:0007744|PDB:5DYS, ECO:0007744|PDB:5EN0, ECO:0007744|PDB:5TE3

Chain	Residue	Details
R	ASN15

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