Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1TAD

GTPASE MECHANISM OF GPROTEINS FROM THE 1.7-ANGSTROM CRYSTAL STRUCTURE OF TRANSDUCIN ALPHA-GDP-ALF4-

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000035	molecular_function	acyl binding
A	0000166	molecular_function	nucleotide 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	0000035	molecular_function	acyl binding
B	0000166	molecular_function	nucleotide binding
B	0001664	molecular_function	G protein-coupled receptor binding
B	0001750	cellular_component	photoreceptor outer segment
B	0001917	cellular_component	photoreceptor inner segment
B	0003924	molecular_function	GTPase activity
B	0005515	molecular_function	protein binding
B	0005525	molecular_function	GTP 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	0007188	biological_process	adenylate cyclase-modulating G protein-coupled receptor signaling pathway
B	0007601	biological_process	visual perception
B	0007602	biological_process	phototransduction
B	0007603	biological_process	phototransduction, visible light
B	0009416	biological_process	response to light stimulus
B	0016020	cellular_component	membrane
B	0019001	molecular_function	guanyl nucleotide binding
B	0019003	molecular_function	GDP binding
B	0019901	molecular_function	protein kinase binding
B	0031683	molecular_function	G-protein beta/gamma-subunit complex binding
B	0042622	cellular_component	photoreceptor outer segment membrane
B	0042995	cellular_component	cell projection
B	0046872	molecular_function	metal ion binding
B	0050908	biological_process	detection of light stimulus involved in visual perception
B	0051344	biological_process	negative regulation of cyclic-nucleotide phosphodiesterase activity
B	0097381	cellular_component	photoreceptor disc membrane
B	0097648	cellular_component	G protein-coupled receptor complex
C	0000035	molecular_function	acyl binding
C	0000166	molecular_function	nucleotide binding
C	0001664	molecular_function	G protein-coupled receptor binding
C	0001750	cellular_component	photoreceptor outer segment
C	0001917	cellular_component	photoreceptor inner segment
C	0003924	molecular_function	GTPase activity
C	0005515	molecular_function	protein binding
C	0005525	molecular_function	GTP binding
C	0005737	cellular_component	cytoplasm
C	0005834	cellular_component	heterotrimeric G-protein complex
C	0007165	biological_process	signal transduction
C	0007186	biological_process	G protein-coupled receptor signaling pathway
C	0007188	biological_process	adenylate cyclase-modulating G protein-coupled receptor signaling pathway
C	0007601	biological_process	visual perception
C	0007602	biological_process	phototransduction
C	0007603	biological_process	phototransduction, visible light
C	0009416	biological_process	response to light stimulus
C	0016020	cellular_component	membrane
C	0019001	molecular_function	guanyl nucleotide binding
C	0019003	molecular_function	GDP binding
C	0019901	molecular_function	protein kinase binding
C	0031683	molecular_function	G-protein beta/gamma-subunit complex binding
C	0042622	cellular_component	photoreceptor outer segment membrane
C	0042995	cellular_component	cell projection
C	0046872	molecular_function	metal ion binding
C	0050908	biological_process	detection of light stimulus involved in visual perception
C	0051344	biological_process	negative regulation of cyclic-nucleotide phosphodiesterase activity
C	0097381	cellular_component	photoreceptor disc membrane
C	0097648	cellular_component	G protein-coupled receptor complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 352

Chain	Residue
A	SER43
A	THR177
A	GDP351
A	ALF355
A	HOH401
A	HOH402

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CAC A 353

Chain	Residue
B	ILE180
A	CYS62
A	VAL164
A	PRO165

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CAC A 354

Chain	Residue
A	ILE180
A	VAL197
A	TRP207
A	CYS210

site_id	AC4
Number of Residues	16
Details	BINDING SITE FOR RESIDUE ALF A 355

Chain	Residue
A	ALA37
A	GLY38
A	GLU39
A	LYS42
A	ARG174
A	LYS176
A	THR177
A	VAL197
A	GLY198
A	GLY199
A	GLN200
A	GDP351
A	CA352
A	HOH400
A	HOH401
A	HOH402

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 352

Chain	Residue
B	SER43
B	THR177
B	GDP351
B	ALF355
B	HOH404
B	HOH405

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CAC B 353

Chain	Residue
B	CYS62
B	VAL164
B	PRO165

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CAC B 354

Chain	Residue
B	VAL197
B	TRP207
B	CYS210

site_id	AC8
Number of Residues	16
Details	BINDING SITE FOR RESIDUE ALF B 355

Chain	Residue
B	ALA37
B	GLY38
B	GLU39
B	LYS42
B	ARG174
B	LYS176
B	THR177
B	VAL197
B	GLY198
B	GLY199
B	GLN200
B	GDP351
B	CA352
B	HOH403
B	HOH404
B	HOH405

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA C 352

Chain	Residue
C	SER43
C	THR177
C	GDP351
C	ALF355
C	HOH407
C	HOH408

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CAC C 353

Chain	Residue
C	CYS62
C	VAL164
C	PRO165
C	HOH904

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CAC C 354

Chain	Residue
C	ILE180
C	VAL197
C	TRP207
C	CYS210

site_id	BC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE ALF C 355

Chain	Residue
C	GLY38
C	GLU39
C	LYS42
C	ARG174
C	LYS176
C	THR177
C	VAL197
C	GLY198
C	GLY199
C	GLN200
C	GDP351
C	CA352
C	HOH406
C	HOH407
C	HOH408

site_id	BC4
Number of Residues	26
Details	BINDING SITE FOR RESIDUE GDP A 351

Chain	Residue
A	ASN265
A	LYS266
A	ASP268
A	VAL269
A	CYS321
A	ALA322
A	THR323
A	CA352
A	ALF355
A	HOH401
A	HOH412
A	HOH414
A	HOH464
A	HOH1000
A	GLU39
A	SER40
A	GLY41
A	LYS42
A	SER43
A	THR44
A	ASP146
A	SER147
A	LEU171
A	ARG172
A	SER173
A	ARG174

site_id	BC5
Number of Residues	27
Details	BINDING SITE FOR RESIDUE GDP B 351

Chain	Residue
B	GLU39
B	SER40
B	GLY41
B	LYS42
B	SER43
B	THR44
B	ASP146
B	SER147
B	LEU171
B	ARG172
B	SER173
B	ARG174
B	ASN265
B	LYS266
B	ASP268
B	VAL269
B	CYS321
B	ALA322
B	THR323
B	CA352
B	ALF355
B	HOH405
B	HOH516
B	HOH517
B	HOH519
B	HOH1165
B	HOH1260

site_id	BC6
Number of Residues	26
Details	BINDING SITE FOR RESIDUE GDP C 351

Chain	Residue
C	GLU39
C	SER40
C	GLY41
C	LYS42
C	SER43
C	THR44
C	ASP146
C	SER147
C	LEU171
C	ARG172
C	SER173
C	ARG174
C	ASN265
C	LYS266
C	ASP268
C	VAL269
C	CYS321
C	ALA322
C	THR323
C	CA352
C	ALF355
C	HOH408
C	HOH592
C	HOH596
C	HOH892
C	HOH942

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	39
Details	Region: {"description":"G1 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	24
Details	Region: {"description":"G2 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	27
Details	Region: {"description":"G3 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	21
Details	Region: {"description":"G4 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	15
Details	Region: {"description":"G5 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	42
Details	Binding site: {"evidences":[{"source":"PubMed","id":"7969474","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8208289","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8259210","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1FQJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FQK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GOT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TAD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TAG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TND","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3V00","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8259210","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1TND","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	9
Details	Binding site: {"evidences":[{"source":"PubMed","id":"7969474","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8208289","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8259210","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1GOT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TAD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TAG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TND","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	3
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P11488","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1ksj

Chain	Residue	Details
A	THR177
A	GLN200
A	GLU39
A	ARG174

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1ksj

Chain	Residue	Details
B	THR177
B	GLN200
B	GLU39
B	ARG174

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

Chain	Residue	Details
C	THR177
C	GLN200
C	GLU39
C	ARG174

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

Chain	Residue	Details
A	GLN200

site_id	CSA5
Number of Residues	1
Details	Annotated By Reference To The Literature 1ksj

Chain	Residue	Details
B	GLN200

site_id	CSA6
Number of Residues	1
Details	Annotated By Reference To The Literature 1ksj

Chain	Residue	Details
C	GLN200

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)