Research workbench

Human AMYLIN2 receptor in complex with gs and salmon calcitonin peptide

Analyse Human AMYLIN2 receptor in complex with gs and salmon calcitonin peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7TYY
Type: protein
Length: 1,250 residues
Chains: 7
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Receptor activity-modifying protein 2; Calcitonin-1; Calcitonin receptor; Guanine…
UniProt: O60895, B5XGR7, P30988, P63092, P62873, P59768
Ligands: PLM, Y01, NAG, NH2
Pockets: 20 · best druggability 0.79

Structure

electron microscopy · 7 distinct chains · 39% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
E	Receptor activity-modifying protein 2	protein	101	71% helix, 0% strand	O60895
P	Calcitonin-1	protein	32	50% helix, 3% strand	B5XGR7
R	Calcitonin receptor	protein	369	66% helix, 7% strand	P30988
A	Guanine nucleotide-binding protein G(S) subunit alpha isoforms short	protein	229	44% helix, 16% strand	P63092
B	Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1	protein	338	8% helix, 43% strand	P62873
G	Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2	protein	54	50% helix, 0% strand	P59768
N	Nanobody 35	protein	127	2% helix, 46% strand	—

Ligands and binding sites

PLM · Palmitic acid · ligand · 5 copies · chains R
Y01 · Cholesterol hemisuccinate · ligand · 2 copies · chains R
NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains R
NH2 · Amino group · ion · chains P, R

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	532	0.79	0.86	52	empty
2	1062	0.78	0.80	61	empty
3	504	0.75	0.83	53	empty
4	763	0.75	0.80	65	empty
5	81	0.66	0.92	23	empty

Interfaces

9 interfaces between chains.

B–G · 2240 Å² buried · 20 hydrogen bonds · protein-protein
P–R · 2062 Å² buried · 18 hydrogen bonds · protein-protein
A–B · 1560 Å² buried · 27 hydrogen bonds · protein-protein
R–A · 1211 Å² buried · 11 hydrogen bonds · protein-protein
A–N · 1034 Å² buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 9 disulfide, 1 glycan (disulfide, N-glycosylation).

Compared structures

7TYY · Human Amylin2 Receptor in complex with Gs and salmon calcitonin peptide · the same entry in another collection · chain N against N, TM-score 1.00
P62873 · AlphaFold monomer V2.0 prediction for guanine nucleotide-binding protein G(I)/G(S)/G(T)… · a predicted model of the same protein · chain B against A, TM-score 0.99
P59768 · AlphaFold monomer V2.0 prediction for guanine nucleotide-binding protein G(I)/G(S)/G(O)… · a predicted model of the same protein · chain G against A, TM-score 0.94
P30988 · AlphaFold monomer V2.0 prediction for calcitonin receptor (P30988) · a predicted model of the same protein · chain R against A, TM-score 0.85
O60895 · AlphaFold monomer V2.0 prediction for receptor activity-modifying protein 2 (O60895) · a predicted model of the same protein · chain E against A, TM-score 0.69

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt O60895
Every structure of UniProt B5XGR7
Every structure of UniProt P30988
Every structure of UniProt P63092
Every structure of UniProt P62873
Every structure of UniProt P59768
Elsewhere: RCSB PDB 7TYY · PDBe 7TYY · UniProt O60895 · UniProt B5XGR7 · UniProt P30988 · UniProt P63092 · UniProt P62873 · UniProt P59768

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