MolNFT v1 · #166600 · protein

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

6UVA · Guanine nucleotide-binding protein G(S) subunit alpha…: “Cryoem structure of the active adrenomedullin 2 receptor G protein complex with adrenomedullin 2 peptide”. Electron microscopy, 17 pockets (best druggability 0.84). MolNFT v1…

PDB: 6UVA
Type: protein
Length: 1,199 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, O60896, Q7Z4H4, Q16602
Pockets: 17 · best druggability 0.84

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	43% helix, 21% strand	P63092
B	Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1	protein	336	6% helix, 47% strand	P62873
G	Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2	protein	49	43% helix, 0% strand	P59768
N	Nanobody 35	protein	126	5% helix, 40% strand	—
E	Receptor activity-modifying protein 3	protein	111	55% helix, 0% strand	O60896
P	Protein ADM2	protein	43	28% helix, 0% strand	Q7Z4H4
R	Calcitonin gene-related peptide type 1 receptor	protein	344	65% helix, 4% strand	Q16602

Pockets

17 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	798	0.84	0.86	77	empty
2	1027	0.78	0.80	66	empty
3	467	0.74	0.83	59	empty
4	669	0.72	0.79	55	empty
5	416	0.61	0.76	30	empty

Interfaces

9 interfaces between chains.

P–R · 2437 Å² buried · 27 hydrogen bonds · protein-protein
E–R · 2155 Å² buried · 7 hydrogen bonds · protein-protein
B–G · 2081 Å² buried · 15 hydrogen bonds · protein-protein
A–B · 1584 Å² buried · 32 hydrogen bonds · protein-protein
A–R · 1125 Å² buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 9 disulfide (disulfide).

Compared structures

6UVA · CryoEM Structure of the active Adrenomedullin 2 receptor G protein complex with… · the same entry in another collection · chain R against R, 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 0.89
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 0.85
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 0.76

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 O60896
Every structure of UniProt Q7Z4H4
Every structure of UniProt Q16602
Elsewhere: RCSB PDB 6UVA · PDBe 6UVA · UniProt P63092 · UniProt P62873 · UniProt P59768 · UniProt O60896 · UniProt Q7Z4H4 · UniProt Q16602

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