Q8WXX5: DnaJ homolog subfamily C member 9 (DNAJC9)

DnaJ homolog subfamily C member 9 (DNAJC9) is a 260-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q8WXX5.

Gene
DNAJC9
Organism
Homo sapiens
Length
260 residues
Mean pLDDT
85.4
Model
AF-Q8WXX5-F1 v6
Model created
1 Aug 2025
PDB structures
2

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Model confidence (pLDDT)

The mean pLDDT of this model is 85.4 (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 accurate51%
70 to 90Confident: backbone generally right38%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions6%

What pLDDT means and how to read it

Function

Acts as a dual histone chaperone and heat shock co-chaperone (PubMed:33857403). As a histone chaperone, forms a co-chaperone complex with MCM2 and histone H3-H4 heterodimers; and may thereby assist MCM2 in histone H3-H4 heterodimer recognition and facilitate the assembly of histones into nucleosomes (PubMed:33857403). May also act as a histone co-chaperone together with TONSL (PubMed:33857403). May recruit histone chaperones ASF1A, NASP and SPT2 to histone H3-H4 heterodimers (PubMed:33857403). Also plays a role as co-chaperone of the HSP70 family of molecular chaperone proteins, such as HSPA1A, HSPA1B and HSPA8 (PubMed:17182002, PubMed:33857403). As a co-chaperone, may play a role in the…

Subunit structure

Forms a co-chaperone complex with MCM2 and histone H3.3-H4 heterodimers (PubMed:33857403). Within the complex, interacts (via C-terminus) with MCM2 (via N-terminus); the interaction is histone-dependent (PubMed:33857403). Within the complex, interacts (via C-terminus) with histone H3.3-H4 heterodimers; the interaction is direct (PubMed:33857403). Interacts with histones H4, H3.3, H3.2 and H3.1,…

Subcellular location

Nucleus, Cytoplasm, Cell membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7CIZX-ray1.8 ÅD/H/L=180-249
7CJ0X-ray2.5 ÅA/D=171-249

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