Q9ULB1: Neurexin-1 (NRXN1)

Neurexin-1 (NRXN1) is a 1477-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9ULB1.

Gene
NRXN1
Organism
Homo sapiens
Length
1477 residues
Mean pLDDT
82.1
Model
AF-Q9ULB1-F1 v6
Model created
1 Aug 2025
PDB structures
1

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Model confidence (pLDDT)

The mean pLDDT of this model is 82.1 (confident 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 accurate58%
70 to 90Confident: backbone generally right23%
50 to 70Low: treat with caution4%
Below 50Very low: often disordered regions14%

What pLDDT means and how to read it

Function

Cell surface protein involved in cell-cell-interactions, exocytosis of secretory granules and regulation of signal transmission. Function is isoform-specific. Alpha-type isoforms have a long N-terminus with six laminin G-like domains and play an important role in synaptic signal transmission. Alpha-type isoforms play a role in the regulation of calcium channel activity and Ca(2+)-triggered neurotransmitter release at synapses and at neuromuscular junctions. They play an important role in Ca(2+)-triggered exocytosis of secretory granules in pituitary gland. They may affect their functions at synapses and in endocrine cells via their interactions with proteins from the exocytotic machinery.…

Subunit structure

Interacts (via laminin G-like domain 2 and/or laminin G-like domain 6) with NLGN1 forming a heterotetramer, where one NLGN1 dimer interacts with one NRXN1 dimer. Also interacts (via laminin G-like domain 2 and/or laminin G-like domain 6) with NLGN2, NLGN3 and NLGN4L; interactions with NLGN1, NLGN2, NLGN3 and NLGN4L are calcium-dependent. Interacts (via cytoplasmic C-terminal region) with CASK…

Subcellular location

Presynaptic cell membrane

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6NIDX-ray1.86 ÅD/E/F=1468-1477

More AlphaFold highlights

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