P50402: Emerin (EMD)

Emerin (EMD) is a 254-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P50402.

Gene
EMD
Organism
Homo sapiens
Length
254 residues
Mean pLDDT
60.3
Model
AF-P50402-F1 v6
Model created
1 Aug 2025
PDB structures
6

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Model confidence (pLDDT)

The mean pLDDT of this model is 60.3 (low 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 accurate19%
70 to 90Confident: backbone generally right9%
50 to 70Low: treat with caution25%
Below 50Very low: often disordered regions48%

What pLDDT means and how to read it

Function

Stabilizes and promotes the formation of a nuclear actin cortical network. Stimulates actin polymerization in vitro by binding and stabilizing the pointed end of growing filaments (PubMed:15328537). Inhibits beta-catenin activity by preventing its accumulation in the nucleus. Acts by influencing the nuclear accumulation of beta-catenin through a CRM1-dependent export pathway (PubMed:16858403). Links centrosomes to the nuclear envelope via a microtubule association (PubMed:17785515). Required for proper localization of non-farnesylated prelamin-A/C (PubMed:19323649). Together with NEMP1, contributes to nuclear envelope stiffness in germ cells (PubMed:32923640). EMD and BAF are cooperative…

Subunit structure

Interacts with lamins A and C, BANF1, GMCL, BCLAF1 and YTHDC1/YT521. Interacts with TMEM43; the interaction retains emerin in the nuclear inner membrane. Interacts with SUN1 and SUN2 (By similarity). Interacts with ACTB, SPTAN1, F-actin, CTNNB1 and beta-tubulin. Interacts with TMEM201. Interacts with NEMP1 (PubMed:32923640)

Subcellular location

Nucleus inner membrane, Nucleus outer membrane

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7NDYX-ray1.44 ÅG=2-187
6GHDX-ray2.1 ÅG/H=2-45
6RPRX-ray2.26 ÅG=2-44
1JEINMRA=2-54
2ODCNMRI=2-47
2ODGNMRC=2-47

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