Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6IBB

Crystal structure of the rat isoform of the succinate receptor SUCNR1 (GPR91) in complex with a nanobody

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0002001	biological_process	renin secretion into blood stream
A	0002281	biological_process	macrophage activation involved in immune response
A	0004930	molecular_function	G protein-coupled receptor activity
A	0005886	cellular_component	plasma membrane
A	0007165	biological_process	signal transduction
A	0007186	biological_process	G protein-coupled receptor signaling pathway
A	0016020	cellular_component	membrane
A	0032922	biological_process	circadian regulation of gene expression
A	0038023	molecular_function	signaling receptor activity
A	0042593	biological_process	glucose homeostasis
A	0050729	biological_process	positive regulation of inflammatory response
A	0050921	biological_process	positive regulation of chemotaxis
A	0051592	biological_process	response to calcium ion
A	0060177	biological_process	regulation of angiotensin metabolic process
A	0097009	biological_process	energy homeostasis
C	0002001	biological_process	renin secretion into blood stream
C	0002281	biological_process	macrophage activation involved in immune response
C	0004930	molecular_function	G protein-coupled receptor activity
C	0005886	cellular_component	plasma membrane
C	0007165	biological_process	signal transduction
C	0007186	biological_process	G protein-coupled receptor signaling pathway
C	0016020	cellular_component	membrane
C	0032922	biological_process	circadian regulation of gene expression
C	0038023	molecular_function	signaling receptor activity
C	0042593	biological_process	glucose homeostasis
C	0050729	biological_process	positive regulation of inflammatory response
C	0050921	biological_process	positive regulation of chemotaxis
C	0051592	biological_process	response to calcium ion
C	0060177	biological_process	regulation of angiotensin metabolic process
C	0097009	biological_process	energy homeostasis

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	binding site for residue OLC A 401

Chain	Residue
A	TYR20
A	HOH549

site_id	AC2
Number of Residues	5
Details	binding site for residue OLC A 402

Chain	Residue
A	LEU185
A	THR188
A	ILE246
A	ASN249
A	HOH550

site_id	AC3
Number of Residues	7
Details	binding site for residue OLC A 403

Chain	Residue
A	THR39
A	ALA284
A	ILE288
A	PHE291
A	ARG298
A	VAL32
A	GLY36

site_id	AC4
Number of Residues	9
Details	binding site for residue OLC A 404

Chain	Residue
A	ILE92
A	ARG95
A	TYR96
A	TRP143
A	LEU151
A	MET153
A	LEU154
A	OLC407
C	OLC406

site_id	AC5
Number of Residues	4
Details	binding site for residue OLC A 405

Chain	Residue
A	MET34
A	PHE38
A	CYS70
A	TYR86

site_id	AC6
Number of Residues	8
Details	binding site for residue OLC A 406

Chain	Residue
A	TRP10
A	PRO243
A	MET247
A	CYS263
A	SER264
A	HOH520
C	OLC402
C	OLC407

site_id	AC7
Number of Residues	8
Details	binding site for residue OLC A 407

Chain	Residue
A	LYS49
A	ASN50
A	TRP51
A	ASN60
A	LYS132
A	TRP143
A	OLC404
A	HOH523

site_id	AC8
Number of Residues	9
Details	binding site for residue OLC A 408

Chain	Residue
A	THR155
A	PHE156
A	THR158
A	GLY175
A	ASN176
A	TYR179
A	ILE182
A	LEU190
C	LEU232

site_id	AC9
Number of Residues	6
Details	binding site for residue GOL A 409

Chain	Residue
A	GLU14
A	SER173
A	LYS269
A	ILE273
A	ARG276
A	HOH533

site_id	AD1
Number of Residues	6
Details	binding site for residue H95 A 410

Chain	Residue
A	LYS225
A	ARG228
A	PHE291
A	HIS296
A	PHE297
A	ARG298

site_id	AD2
Number of Residues	9
Details	binding site for residue OLC C 401

Chain	Residue
A	ILE16
A	LEU17
A	TYR20
A	TYR21
C	LEU129
C	PHE134
C	ALA141
C	OLC402
C	OLC408

site_id	AD3
Number of Residues	9
Details	binding site for residue OLC C 402

Chain	Residue
A	SER238
A	VAL239
A	PRO243
A	THR275
A	OLC406
C	LEU140
C	VAL144
C	OLC401
C	OLC407

site_id	AD4
Number of Residues	5
Details	binding site for residue CLR C 403

Chain	Residue
C	PHE111
C	LEU145
C	VAL198
C	OLC408
C	HOH529

site_id	AD5
Number of Residues	9
Details	binding site for residue OLC C 404

Chain	Residue
C	TYR44
C	LEU45
C	MET48
C	LYS49
C	TRP51
C	ASN60
C	LYS132
C	TRP143
C	OLC407

site_id	AD6
Number of Residues	5
Details	binding site for residue OLC C 405

Chain	Residue
C	LYS205
C	OLC406
C	SER197
C	PHE201
C	TYR204

site_id	AD7
Number of Residues	10
Details	binding site for residue OLC C 406

Chain	Residue
A	LEU154
A	OLC404
C	LEU193
C	CYS200
C	TYR203
C	TYR204
C	SER238
C	THR242
C	OLC405
C	HOH547

site_id	AD8
Number of Residues	6
Details	binding site for residue OLC C 407

Chain	Residue
A	OLC406
C	TYR96
C	LEU140
C	TRP143
C	OLC402
C	OLC404

site_id	AD9
Number of Residues	11
Details	binding site for residue OLC C 408

Chain	Residue
C	SER53
C	TYR57
C	PHE111
C	ILE114
C	ASP115
C	LEU118
C	LEU129
C	PHE134
C	OLC401
C	CLR403
C	HOH502

site_id	AE1
Number of Residues	9
Details	binding site for residue GOL C 409

Chain	Residue
C	LYS18
C	VAL169
C	ASP170
C	SER173
C	LYS269
C	ILE273
C	ARG276
C	HOH514
C	HOH518

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	THR104-MET120

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	40
Details	Transmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	55
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	40
Details	Transmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	72
Details	Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	40
Details	Transmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	40
Details	Transmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	40
Details	Transmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	40
Details	Transmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	40
Details	Transmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)