Q9NVP2: Histone chaperone ASF1B (ASF1B)

Histone chaperone ASF1B (ASF1B) is a 202-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9NVP2.

Gene
ASF1B
Organism
Homo sapiens
Length
202 residues
Mean pLDDT
84.6
Model
AF-Q9NVP2-F1 v6
Model created
1 Aug 2025
PDB structures
4

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Model confidence (pLDDT)

The mean pLDDT of this model is 84.6 (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 accurate75%
70 to 90Confident: backbone generally right1%
50 to 70Low: treat with caution6%
Below 50Very low: often disordered regions17%

What pLDDT means and how to read it

Function

Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly (PubMed:11897662, PubMed:14718166, PubMed:15664198, PubMed:16151251, PubMed:21454524, PubMed:26527279). Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly (PubMed:11897662, PubMed:14718166, PubMed:15664198, PubMed:16151251). Also involved in the nuclear import of the histone H3-H4 dimer together with importin-4 (IPO4): specifically recognizes and binds newly synthesized histones with the monomethylation of H3 'Lys-9' (H3K9me1) and diacetylation at 'Lys-5' and 'Lys-12' of H4 (H4K5K12ac) marks in the cytosol…

Subunit structure

Interacts with histone H3 (via C-terminus), including histone H3.1, H3.2 and H3.3, and histone H4; the interaction with H3 is direct (PubMed:12842904, PubMed:14718166, PubMed:15664198, PubMed:16537536, PubMed:22195965). Interacts with the CHAF1A, CHAF1B and RBBP4 subunits of the CAF-1 complex (PubMed:11897662, PubMed:14718166, PubMed:16537536, PubMed:16980972). Interacts with HAT1, NASP and TAF1…

Subcellular location

Nucleus, Cytoplasm, cytosol

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5BNXX-ray2.31 ÅD=1-158
7V1MX-ray2.83 ÅD/F=1-158
5BO0X-ray2.91 ÅD=1-158
7VCQX-ray3.0 ÅD/F/I=1-156

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