P18272: Nucleoprotein (NP)

Nucleoprotein (NP) is a 739-residue protein from Zaire ebolavirus. This is its AlphaFold structure prediction, created 3 Jul 2025. UniProt accession: P18272.

Gene
NP
Organism
Zaire ebolavirus
Length
739 residues
Mean pLDDT
62.4
Model
AF-0000000365763776 v1
Model created
3 Jul 2025
PDB structures
16

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Model confidence (pLDDT)

The mean pLDDT of this model is 62.4 (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 accurate14%
70 to 90Confident: backbone generally right40%
50 to 70Low: treat with caution10%
Below 50Very low: often disordered regions36%

What pLDDT means and how to read it

Function

Oligomerizes into helical capsid to encapsidate the viral genome, protecting it from nucleases and the cellular innate immune response (PubMed:16719918, PubMed:25865894, PubMed:26119732, PubMed:30333622). VP35 binds to and stabilizes monomeric NP, keeping it soluble (PubMed:25865894, PubMed:26119732). Upon virus replication, NP is recruited to bind cooperatively viral genomic RNA and VP35 is released (PubMed:29144446). The encapsidated genomic RNA is termed the nucleocapsid and serves as template for transcription and replication. The nucleocapsid is helical with a pitch of 10.81 NP per turn and a diameter of about 22nm (PubMed:22247782). Each NP binds to six nucleotides of viral genomic…

Subunit structure

Homooligomer. Homomultimerizes to form the nucleocapsid. Binds to viral genomic RNA. Interacts with VP35 and VP30 to form the nucleocapsid (PubMed:12191476, PubMed:25865894, PubMed:25910597, PubMed:26119732, PubMed:27755595). Interacts with host PPP2R5C; this interaction leads to VP30 dephosphorylation and viral transcription (PubMed:29290611). Interacts with VP24; this interaction facilitates…

Subcellular location

Virion, Host cytoplasm

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4QB0X-ray1.75 ÅA=641-739
4Z9PX-ray1.79 ÅA=36-351
4QAZX-ray1.98 ÅA=641-739
5T3TX-ray2.2 ÅA/B/C/D/E/F/G/H/I/J=600-627
4ZTAX-ray2.4 ÅA=34-367
4ZTIX-ray2.4 ÅA/B=34-367
4ZTGX-ray2.8 ÅA=34-367
6NUTEM3.1 ÅA=1-450
4YPIX-ray3.71 ÅA/B/C/D=38-385
5Z9WEM3.9 ÅA=19-406
8Y9JEM4.6 ÅA/B=1-739
6C54EM5.8 ÅA/B=25-457
6EHLEM6.6 ÅA=1-739
6EHMEM7.3 ÅA/B=1-739
8USTEM7.3 ÅA/B/E=1-739
8USNEM8.9 ÅA/B/E=1-739

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