Q15006: ER membrane protein complex subunit 2 (EMC2)

ER membrane protein complex subunit 2 (EMC2) is a 297-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q15006.

Gene
EMC2
Organism
Homo sapiens
Length
297 residues
Mean pLDDT
94.3
Model
AF-Q15006-F1 v6
Model created
1 Aug 2025
PDB structures
11

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Model confidence (pLDDT)

The mean pLDDT of this model is 94.3 (very high overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate85%
70 to 90Confident: backbone generally right13%
50 to 70Low: treat with caution1%
Below 50Very low: often disordered regions0%

What pLDDT means and how to read it

Function

Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins (PubMed:29242231, PubMed:29809151, PubMed:30415835, PubMed:32439656, PubMed:32459176, PubMed:33964204). Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues (PubMed:29242231, PubMed:29809151, PubMed:30415835). Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices (PubMed:29809151,…

Subunit structure

Component of the ER membrane protein complex (EMC) (PubMed:22119785, PubMed:29242231, PubMed:32439656, PubMed:32459176, PubMed:33964204). Interacts with WNK1 (via amphipathic alpha-helix region); promoting the ER membrane protein complex assembly by preventing EMC2 ubiquitination (PubMed:33964204)

Subcellular location

Endoplasmic reticulum membrane

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
6Y4LX-ray2.2 ÅA=11-274
8J0OEM3.32 ÅB=1-297
7ADOEM3.39 ÅB=1-297
6WW7EM3.4 ÅB=1-297
8EOIEM3.4 ÅB=3-293
8J0NEM3.47 ÅB=1-297
7ADPEM3.6 ÅB=1-297
8S9SEM3.6 Å2=1-297
9ZZ6EM4.16 ÅB=1-297
6Z3WEM6.4 ÅB=1-297
9C7VEM6.6 Å2=1-297

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