Binding Site Information of Target

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Target General Information
Drug Binding Sites of Target
References
Target General Information  Top
Target ID T44919 Target Info
Target Name Glucagon (GCG)
Synonyms GRPP; GLP2; GLP1; GLP-1
Target Type Clinical trial Target
Gene Name GCG
Biochemical Class Glucagon
UniProt ID
GLUC_HUMAN
Drug Binding Sites of Target  Top
Ligand Name: L-glutamic acid Ligand Info
Structure Description Solution structure of lipidated glucagon analog in water PDB:2M5P
Method Solution NMR Resolution N.A. Mutation Yes [1]
PDB Sequence
HQGTFTSDYS
11
KKLDRRAQDF
22
VQWLMNT
Residue
Distance (Å)
GLN3
3.808
GLY4
3.792
THR5
2.984
SER8
2.347
LYS12
1.686
Residue
Distance (Å)
LYS13
1.325
LEU14
4.063
ASP15
4.413
ARG17
1.851
ARG18
2.976
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Ligand Name: Alpha-Aminoisobutyric Acid Ligand Info
Structure Description Semaglutide-bound Glucagon-Like Peptide-1 (GLP-1) Receptor in Complex with Gs protein PDB:7KI0
Method Electron microscopy Resolution 2.50 Å Mutation No [2]
PDB Sequence
HEGTFTSDVS
17
SYLEGQAAKE
27
FIAWLVRGR
Residue
Distance (Å)
HIS7
1.338
GLU9
1.339
GLY10
3.352
Residue
Distance (Å)
THR11
3.044
PHE12
2.820
THR13
4.818
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Ligand Name: Palmitoyl glutamic acid Ligand Info
Structure Description Liraglutide PDB:4APD
Method Solution NMR Resolution N.A. Mutation Yes [3]
PDB Sequence
HAEGTFTSDV
16
SSYLEGQAAK
26
EFIAWLVRGR
36
G
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .D6M or .D6M2 or .D6M3 or :3D6M;style chemicals stick;color identity;select .A:22 or .A:25 or .A:26 or .A:28 or .A:29 or .A:31 or .A:32 or .A:33 or .A:36; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY22
4.728
ALA25
2.306
LYS26
1.328
PHE28
1.896
ILE29
1.974
Residue
Distance (Å)
TRP31
1.961
LEU32
1.987
VAL33
2.040
ARG36
4.122
Ligand Name: 3,6,9,12,15,18-Hexaoxahexacosan-1-ol Ligand Info
Structure Description Crystal structure of Semaglutide peptide backbone in complex with the GLP-1 receptor extracellular domain PDB:4ZGM
Method X-ray diffraction Resolution 1.80 Å Mutation No [4]
PDB Sequence
GTFTSDVSSY
19
LEGQAAKEFI
29
AWLVRGRG
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set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .32M or .32M2 or .32M3 or :332M;style chemicals stick;color identity;select .B:20 or .B:21 or .B:23 or .B:24 or .B:25 or .B:27 or .B:28 or .B:31 or .B:34 or .B:36; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU20
2.570
GLU21
4.601
GLN23
2.853
ALA24
2.030
ALA25
4.763
Residue
Distance (Å)
GLU27
2.110
PHE28
2.118
TRP31
2.731
ARG34
3.876
ARG36
2.476
Ligand Name: 2-[2-[2-[[2-[2-(2-Aminoethoxy)ethoxy]acetyl]amino]ethoxy]ethoxy]acetic acid Ligand Info
Structure Description Semaglutide-bound Glucagon-Like Peptide-1 (GLP-1) Receptor in Complex with Gs protein PDB:7KI0
Method Electron microscopy Resolution 2.50 Å Mutation No [2]
PDB Sequence
HEGTFTSDVS
17
SYLEGQAAKE
27
FIAWLVRGR
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set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .WF1 or .WF12 or .WF13 or :3WF1;style chemicals stick;color identity;select .P:19 or .P:23 or .P:26 or .P:27; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
TYR19
4.274
GLN23
3.344
Residue
Distance (Å)
LYS26
1.450
GLU27
3.226
Ligand Name: 1-[(1R)-1-(2,6-dichloro-3-methoxyphenyl)ethyl]-6-{2-[(2R)-piperidin-2-yl]phenyl}-1H-benzimidazole Ligand Info
Structure Description Cryo-EM structure of the Glucagon-like peptide-1 receptor in complex with G protein, GLP-1 peptide and a positive allosteric modulator PDB:6VCB
Method Electron microscopy Resolution 3.30 Å Mutation Yes [5]
PDB Sequence
HAEGTFTSDV
16
SSYLEGQAAK
26
EFIAWLVKGR
36
G
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .QW7 or .QW72 or .QW73 or :3QW7;style chemicals stick;color identity;select .P:12 or .P:16 or .P:20; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE12
4.530
VAL16
3.854
Residue
Distance (Å)
LEU20
3.235
Ligand Name: {(8R,9S,10S)-9-(2',3'-dimethyl[1,1'-biphenyl]-4-yl)-6-[(1-methyl-1H-imidazol-2-yl)sulfonyl]-1,6-diazabicyclo[6.2.0]decan-10-yl}methanol Ligand Info
Structure Description Structure of Cysteine-free Human Insulin-Degrading Enzyme in complex with Glucagon and Substrate-selective Macrocyclic Inhibitor 63 PDB:6EDS
Method X-ray diffraction Resolution 3.18 Å Mutation Yes [6]
PDB Sequence
HSQGTFVQWL
26
MN
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set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .J22 or .J222 or .J223 or :3J22;style chemicals stick;color identity;select .C:3 or .C:4 or .C:5 or .C:22; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLN3
2.766
GLY4
4.195
Residue
Distance (Å)
THR5
2.781
PHE22
2.648
References  Top
REF 1 Structural Changes Associated with Peptide Lipidation Broaden Biological Function
REF 2 Structure and dynamics of semaglutide- and taspoglutide-bound GLP-1R-Gs complexes. Cell Rep. 2021 Jul 13;36(2):109374.
REF 3 Liraglutide
REF 4 Discovery of the Once-Weekly Glucagon-Like Peptide-1 (GLP-1) Analogue Semaglutide. J Med Chem. 2015 Sep 24;58(18):7370-80.
REF 5 Structural insights into probe-dependent positive allosterism of the GLP-1 receptor. Nat Chem Biol. 2020 Oct;16(10):1105-1110.
REF 6 Substrate-selective inhibitors that reprogram the activity of insulin-degrading enzyme. Nat Chem Biol. 2019 Jun;15(6):565-574.

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