Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5VEW

Structure of the human GLP-1 receptor complex with PF-06372222

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003796	molecular_function	lysozyme activity
A	0003824	molecular_function	catalytic 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	0016787	molecular_function	hydrolase activity
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	0003824	molecular_function	catalytic 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	0016787	molecular_function	hydrolase activity
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	12
Details	binding site for residue 97Y A 1201

Chain	Residue
A	VAL331
A	OLC1203
B	ILE286
B	OLC1201
A	PHE347
A	ARG348
A	LYS351
A	SER352
A	THR355
A	LEU401
A	VAL405
A	ASN406

site_id	AC2
Number of Residues	7
Details	binding site for residue OLC A 1202

Chain	Residue
A	SER163
A	TYR178
A	LEU181
A	ASN182
A	ILE188
A	PHE266
A	OLA1204

site_id	AC3
Number of Residues	2
Details	binding site for residue OLC A 1203

Chain	Residue
A	LYS342
A	97Y1201

site_id	AC4
Number of Residues	2
Details	binding site for residue OLA A 1204

Chain	Residue
A	HIS173
A	OLC1202

site_id	AC5
Number of Residues	6
Details	binding site for residue OLC B 1201

Chain	Residue
A	PHE324
A	THR362
A	97Y1201
B	LEU278
B	LEU279
B	VAL282

site_id	AC6
Number of Residues	13
Details	binding site for residue 97Y B 1202

Chain	Residue
A	ILE286
B	VAL331
B	PHE347
B	ARG348
B	LYS351
B	SER352
B	THR355
B	MET397
B	LEU401
B	VAL405
B	ASN406
B	OLC1203
B	OLC1205

site_id	AC7
Number of Residues	6
Details	binding site for residue OLC B 1203

Chain	Residue
A	LEU278
A	LEU279
A	VAL282
B	THR362
B	GLU387
B	97Y1202

site_id	AC8
Number of Residues	4
Details	binding site for residue OLC B 1204

Chain	Residue
B	SER163
B	TYR178
B	ASN182
B	PHE266

site_id	AC9
Number of Residues	2
Details	binding site for residue OLC B 1205

Chain	Residue
B	LYS342
B	97Y1202

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	2
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04110","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"3382407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04110","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1892846","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3382407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	48
Details	Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"28514449","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	58
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"28514449","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	50
Details	Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"28514449","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	48
Details	Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"28514449","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	28
Details	Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"28514449","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	44
Details	Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"28514449","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	40
Details	Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"28514449","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	6
Details	Region: {"description":"Important for allosteric inhibitor binding","evidences":[{"source":"PubMed","id":"28514449","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	2
Details	Modified residue: {"description":"ADP-ribosylcysteine","evidences":[{"source":"PubMed","id":"21901419","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	2
Details	Modified residue: {"description":"ADP-ribosylarginine","evidences":[{"source":"PubMed","id":"21901419","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	2
Details	M-CSA 921

Chain	Residue	Details
A	LEU1015	proton shuttle (general acid/base)
A	TYR1024	covalent catalysis

site_id	MCSA2
Number of Residues	2
Details	M-CSA 921

Chain	Residue	Details
B	LEU1015	proton shuttle (general acid/base)
B	TYR1024	covalent catalysis

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