Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5EE7

Crystal structure of the human glucagon receptor (GCGR) in complex with the antagonist MK-0893

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	binding site for residue 5MV A 1201

Chain	Residue
A	GLY269
A	SER350
A	THR353
A	LEU399
A	ASN404
A	LYS405
A	OLA1211
A	OLA1212
A	OLA1214
A	HOH1313
A	ILE270
A	GLY273
A	ALA274
A	LEU277
A	LEU329
A	PHE345
A	ARG346
A	LYS349

site_id	AC2
Number of Residues	2
Details	binding site for residue OLA A 1202

Chain	Residue
A	LEU268
A	OLA1214

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

Chain	Residue
A	PHE289
A	ALA380

site_id	AC4
Number of Residues	4
Details	binding site for residue OLA A 1204

Chain	Residue
A	HIS361
A	ASP385
A	LEU388
A	PHE391

site_id	AC5
Number of Residues	8
Details	binding site for residue OLA A 1205

Chain	Residue
A	THR146
A	SER150
A	PHE320
A	VAL323
A	ARG324
A	GLN327
A	OLA1206
A	OLA1209

site_id	AC6
Number of Residues	3
Details	binding site for residue OLA A 1206

Chain	Residue
A	ARG324
A	OLA1205
A	HOH1309

site_id	AC7
Number of Residues	2
Details	binding site for residue OLA A 1207

Chain	Residue
A	SER189
A	VAL326

site_id	AC8
Number of Residues	4
Details	binding site for residue OLA A 1208

Chain	Residue
A	CYS171
A	THR172
A	ASN179
A	PHE264

site_id	AC9
Number of Residues	4
Details	binding site for residue OLA A 1209

Chain	Residue
A	HIS250
A	ILE317
A	ARG324
A	OLA1205

site_id	AD1
Number of Residues	3
Details	binding site for residue OLA A 1210

Chain	Residue
A	ASP218
A	ARG225
A	LYS1058

site_id	AD2
Number of Residues	2
Details	binding site for residue OLA A 1211

Chain	Residue
A	5MV1201
A	OLA1212

site_id	AD3
Number of Residues	4
Details	binding site for residue OLA A 1212

Chain	Residue
A	PHE345
A	5MV1201
A	OLA1211
A	OLA1213

site_id	AD4
Number of Residues	3
Details	binding site for residue OLA A 1213

Chain	Residue
A	LEU352
A	OLA1212
A	OLA1215

site_id	AD5
Number of Residues	4
Details	binding site for residue OLA A 1214

Chain	Residue
A	SER265
A	5MV1201
A	OLA1202
A	HOH1301

site_id	AD6
Number of Residues	3
Details	binding site for residue OLA A 1215

Chain	Residue
A	LEU333
A	ARG334
A	OLA1213

site_id	AD7
Number of Residues	13
Details	binding site for residue PE5 A 1216

Chain	Residue
A	TYR145
A	TYR149
A	LYS187
A	ILE194
A	ARG199
A	ILE235
A	ASN238
A	TYR239
A	THR296
A	MET301
A	HIS361
A	PHE365
A	GLN392

site_id	AD8
Number of Residues	7
Details	binding site for residue TLA A 1217

Chain	Residue
A	ILE315
A	ASN318
A	PHE319
A	ILE355
A	PRO356
A	GLY359
A	VAL360

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. QGLLVaVLYCFlNkeV

Chain	Residue	Details
A	GLN392-VAL407

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
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	1
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	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	34
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"23863937","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27111510","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28514451","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	24
Details	Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"23863937","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27111510","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28514451","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	23
Details	Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"23863937","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27111510","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28514451","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	21
Details	Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"23863937","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27111510","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28514451","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	22
Details	Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"23863937","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27111510","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28514451","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	18
Details	Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"23863937","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27111510","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28514451","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"23863937","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27111510","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28514451","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	3
Details	Region: {"description":"Important for allosteric inhibitor binding","evidences":[{"source":"PubMed","id":"27111510","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28514451","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	GLU1009	proton shuttle (general acid/base)
A	ASP1018	covalent catalysis

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