MolNFT v2 · #180072 · protein

Cryo-EM structure of human GPR158 in complex with RGS7-Gbeta5 in a 2:1:1 ratio

7EWP: “Cryo-EM structure of human GPR158 in complex with RGS7-Gbeta5 in a 2:1:1 ratio”. Electron microscopy at 4.3. MolNFT v2 #180072 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7EWP
Type: protein
Length: 1,816 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 4.3
Source: Homo sapiens
UniProt: Q5T848, P49802, O14775

Structure

electron microscopy · resolution 4.3 · 4 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	577	—	Q5T848
B	—	protein	504	—	Q5T848
C	—	protein	396	—	P49802
D	—	protein	339	—	O14775

Compared structures

7EWP · Cryo-EM structure of human GPR158 in complex with RGS7-GBETA5 in a 2:1:1 ratio · the same entry in another collection · chain D against D, TM-score 1.00
P49802 · AlphaFold monomer V2.0 prediction for regulator of G-protein signaling 7 (P49802) · a predicted model of the same protein · chain C against A, TM-score 0.96
O14775 · AlphaFold monomer V2.0 prediction for guanine nucleotide-binding protein subunit beta-5… · a predicted model of the same protein · chain D against A, TM-score 0.95
Q5T848 · AlphaFold monomer V2.0 prediction for probable G-protein coupled receptor 158 (Q5T848) · a predicted model of the same protein · chain B against A, TM-score 0.83

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 Q5T848
Every structure of UniProt P49802
Every structure of UniProt O14775
Elsewhere: RCSB PDB 7EWP · PDBe 7EWP · UniProt Q5T848 · UniProt P49802 · UniProt O14775

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