Research workbench

Cryoem structure of the active adrenomedullin 2 receptor G protein complex with adrenomedullin peptide

Analyse Cryoem structure of the active adrenomedullin 2 receptor G protein complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6UUS
Type: protein
Length: 1,190 residues
Chains: 7
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Guanine nucleotide-binding protein G(S) subunit alpha isoforms short; Guanine…
UniProt: P63092, P62873, P59768, P35318, Q16602, O60896
Pockets: 20 · best druggability 0.82

Structure

electron microscopy · 7 distinct chains · 35% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Guanine nucleotide-binding protein G(S) subunit alpha isoforms short	protein	190	42% helix, 21% strand	P63092
B	Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1	protein	336	5% helix, 47% strand	P62873
G	Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2	protein	49	53% helix, 0% strand	P59768
N	Nanobody 35	protein	126	2% helix, 43% strand	—
P	Adm	protein	37	30% helix, 0% strand	P35318
R	Calcitonin gene-related peptide type 1 receptor	protein	341	65% helix, 3% strand	Q16602
E	Receptor activity-modifying protein 3	protein	111	58% helix, 0% strand	O60896

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	703	0.82	0.86	58	empty
2	965	0.78	0.80	62	empty
3	671	0.72	0.79	49	empty
4	355	0.68	0.81	44	empty
5	100	0.67	0.91	26	empty

Interfaces

9 interfaces between chains.

B–G · 2078 Å² buried · 14 hydrogen bonds · protein-protein
P–R · 2050 Å² buried · 16 hydrogen bonds · protein-protein
R–E · 1880 Å² buried · 5 hydrogen bonds · protein-protein
A–B · 1552 Å² buried · 31 hydrogen bonds · protein-protein
A–R · 1136 Å² buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 9 disulfide (disulfide).

Compared structures

6UUS · CryoEM Structure of the active Adrenomedullin 2 receptor G protein complex with… · the same entry in another collection · chain E against E, 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 0.91
Q16602 · AlphaFold monomer V2.0 prediction for calcitonin gene-related peptide type 1 receptor… · a predicted model of the same protein · chain R against A, TM-score 0.83
P63092 · AlphaFold monomer V2.0 prediction for guanine nucleotide-binding protein G(S) subunit… · a predicted model of the same protein · chain A against A, TM-score 0.83
O60896 · AlphaFold monomer V2.0 prediction for receptor activity-modifying protein 3 (O60896) · a predicted model of the same protein · chain E against A, TM-score 0.80

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 P63092
Every structure of UniProt P62873
Every structure of UniProt P59768
Every structure of UniProt P35318
Every structure of UniProt Q16602
Every structure of UniProt O60896
Elsewhere: RCSB PDB 6UUS · PDBe 6UUS · UniProt P63092 · UniProt P62873 · UniProt P59768 · UniProt P35318 · UniProt Q16602 · UniProt O60896

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.