P55209: Nucleosome assembly protein 1-like 1 (NAP1L1)

Nucleosome assembly protein 1-like 1 (NAP1L1) is a 391-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P55209.

Gene
NAP1L1
Organism
Homo sapiens
Length
391 residues
Mean pLDDT
79.9
Model
AF-P55209-F1 v6
Model created
1 Aug 2025
PDB structures
3

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Model confidence (pLDDT)

The mean pLDDT of this model is 79.9 (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 accurate54%
70 to 90Confident: backbone generally right15%
50 to 70Low: treat with caution18%
Below 50Very low: often disordered regions14%

What pLDDT means and how to read it

Function

Histone chaperone that plays a role in the nuclear import of H2A-H2B and nucleosome assembly (PubMed:20002496, PubMed:21211722, PubMed:26841755). Also participates in several important DNA repair mechanisms: greatly enhances ERCC6-mediated chromatin remodeling which is essential for transcription-coupled nucleotide excision DNA repair (PubMed:28369616). Also stimulates homologous recombination (HR) by RAD51 and RAD54 which is essential in mitotic DNA double strand break (DSB) repair (PubMed:24798879). Plays a key role in the regulation of embryonic neurogenesis (By similarity). Promotes the proliferation of neural progenitors and inhibits neuronal differentiation during cortical…

Subunit structure

Homodimer (PubMed:26841755). The dimer binds strongly and sequentially to single and double H2A-H2B heterodimers (PubMed:26841755). Interacts with ERCC6; this interaction increases ERCC6 processivity (PubMed:28369616). Interacts with RAD54 (PubMed:24798879). Interacts with SETD1A (By similarity)

Subcellular location

Nucleus, Chromosome, Melanosome, Cytoplasm

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7BP5X-ray1.9 ÅC=371-377
7UN6EM3.3 ÅB/C=2-391
7UN3EM3.5 ÅB/C=2-391

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