Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6KK1

Structure of thermal-stabilised(M8) human GLP-1 receptor transmembrane domain

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003796	molecular_function	lysozyme activity
A	0004888	molecular_function	transmembrane signaling receptor activity
A	0004930	molecular_function	G protein-coupled receptor activity
A	0007166	biological_process	cell surface receptor signaling pathway
A	0007186	biological_process	G protein-coupled receptor signaling pathway
A	0009253	biological_process	peptidoglycan catabolic process
A	0016020	cellular_component	membrane
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0016998	biological_process	cell wall macromolecule catabolic process
A	0030430	cellular_component	host cell cytoplasm
A	0031640	biological_process	killing of cells of another organism
A	0042742	biological_process	defense response to bacterium
A	0044659	biological_process	viral release from host cell by cytolysis
B	0003796	molecular_function	lysozyme activity
B	0004888	molecular_function	transmembrane signaling receptor activity
B	0004930	molecular_function	G protein-coupled receptor activity
B	0007166	biological_process	cell surface receptor signaling pathway
B	0007186	biological_process	G protein-coupled receptor signaling pathway
B	0009253	biological_process	peptidoglycan catabolic process
B	0016020	cellular_component	membrane
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0016998	biological_process	cell wall macromolecule catabolic process
B	0030430	cellular_component	host cell cytoplasm
B	0031640	biological_process	killing of cells of another organism
B	0042742	biological_process	defense response to bacterium
B	0044659	biological_process	viral release from host cell by cytolysis

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	binding site for residue 97Y A 2001

Chain	Residue
A	VAL331
A	ASN406
B	ILE286
A	PHE347
A	ARG348
A	LYS351
A	SER352
A	LEU354
A	THR355
A	LEU401
A	VAL405

site_id	AC2
Number of Residues	10
Details	binding site for residue 97Y B 2001

Chain	Residue
A	ILE286
B	VAL331
B	PHE347
B	ARG348
B	LYS351
B	SER352
B	THR355
B	LEU401
B	VAL405
B	ASN406

Functional Information from PROSITE/UniProt

site_id	PS00650
Number of Residues	16
Details	G_PROTEIN_RECEP_F2_2 G-protein coupled receptors family 2 signature 2. QGLMVaILYCFvNneV

Chain	Residue	Details
A	GLN394-VAL409

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	48
Details	TRANSMEM: Helical; Name=1 => ECO:0000269\|PubMed:28514449

Chain	Residue	Details
A	GLN140-ALA164
B	GLN140-ALA164

site_id	SWS_FT_FI2
Number of Residues	58
Details	TOPO_DOM: Cytoplasmic => ECO:0000269\|PubMed:28514449

Chain	Residue	Details
A	ILE165-THR175
A	CYS329-ARG348
B	ILE165-THR175
B	CYS329-ARG348

site_id	SWS_FT_FI3
Number of Residues	50
Details	TRANSMEM: Helical; Name=2 => ECO:0000269\|PubMed:28514449

Chain	Residue	Details
A	ARG176-LEU201
B	ARG176-LEU201

site_id	SWS_FT_FI4
Number of Residues	102
Details	TOPO_DOM: Extracellular => ECO:0000269\|PubMed:28514449

Chain	Residue	Details
A	LYS202-GLN234
A	TYR291-TYR305
A	MET371-LYS383
B	LYS202-GLN234
B	TYR291-TYR305
B	MET371-LYS383

site_id	SWS_FT_FI5
Number of Residues	46
Details	TRANSMEM: Helical; Name=3 => ECO:0000269\|PubMed:28514449

Chain	Residue	Details
A	LEU228-LEU251
B	LEU228-LEU251

site_id	SWS_FT_FI6
Number of Residues	48
Details	TRANSMEM: Helical; Name=4 => ECO:0000269\|PubMed:28514449

Chain	Residue	Details
A	PHE266-LEU290
B	PHE266-LEU290

site_id	SWS_FT_FI7
Number of Residues	44
Details	TRANSMEM: Helical; Name=5 => ECO:0000269\|PubMed:28514449

Chain	Residue	Details
A	TRP306-ILE328
B	TRP306-ILE328

site_id	SWS_FT_FI8
Number of Residues	42
Details	TRANSMEM: Helical; Name=6 => ECO:0000269\|PubMed:28514449

Chain	Residue	Details
A	LEU349-VAL370
B	LEU349-VAL370

site_id	SWS_FT_FI9
Number of Residues	40
Details	TRANSMEM: Helical; Name=7 => ECO:0000269\|PubMed:28514449

Chain	Residue	Details
A	LEU384-PHE404
B	LEU384-PHE404

site_id	SWS_FT_FI10
Number of Residues	2
Details	SITE: Interaction with the endogenous ligand GLP-1 => ECO:0000269\|PubMed:19861722

Chain	Residue	Details
A	GLU128
B	GLU128

site_id	SWS_FT_FI11
Number of Residues	2
Details	MOD_RES: ADP-ribosylcysteine => ECO:0000269\|PubMed:21901419

Chain	Residue	Details
A	CYS341
B	CYS341

site_id	SWS_FT_FI12
Number of Residues	2
Details	MOD_RES: ADP-ribosylarginine => ECO:0000269\|PubMed:21901419

Chain	Residue	Details
A	ARG348
B	ARG348

site_id	SWS_FT_FI13
Number of Residues	2
Details	ACT_SITE: Proton donor/acceptor => ECO:0000255\|HAMAP-Rule:MF_04110, ECO:0000269\|PubMed:3382407, ECO:0000269\|PubMed:7831309, ECO:0000269\|PubMed:8266098

Chain	Residue	Details
A	GLU1010
B	GLU1010

site_id	SWS_FT_FI14
Number of Residues	2
Details	ACT_SITE: Proton donor/acceptor => ECO:0000255\|HAMAP-Rule:MF_04110, ECO:0000269\|PubMed:1892846, ECO:0000269\|PubMed:3382407, ECO:0000269\|PubMed:7831309, ECO:0000269\|PubMed:8266098

Chain	Residue	Details
A	ASP1019
B	ASP1019

site_id	SWS_FT_FI15
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:8266098

Chain	Residue	Details
A	LEU1031
A	PHE1103
B	LEU1031
B	PHE1103

site_id	SWS_FT_FI16
Number of Residues	4
Details	BINDING: BINDING => ECO:0000303\|PubMed:7831309

Chain	Residue	Details
A	SER1116
A	ASN1131
B	SER1116
B	ASN1131

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	2
Details	M-CSA 921

Chain	Residue	Details
A	GLU1010	proton shuttle (general acid/base)
A	ASP1019	covalent catalysis

site_id	MCSA2
Number of Residues	2
Details	M-CSA 921

Chain	Residue	Details
B	GLU1010	proton shuttle (general acid/base)
B	ASP1019	covalent catalysis

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