P51610: Host cell factor 1 (HCFC1)

Host cell factor 1 (HCFC1) is a 2035-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P51610.

Gene
HCFC1
Organism
Homo sapiens
Length
2035 residues
Mean pLDDT
46.4
Model
AF-P51610-F1 v6
Model created
1 Aug 2025
PDB structures
11

Explore in 3D Color by confidence AlphaFold DB UniProt

Model confidence (pLDDT)

The mean pLDDT of this model is 46.4 (very 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 accurate19%
70 to 90Confident: backbone generally right7%
50 to 70Low: treat with caution2%
Below 50Very low: often disordered regions73%

What pLDDT means and how to read it

Function

Transcriptional coregulator (By similarity). Serves as a scaffold protein, bridging interactions between transcription factors, including THAP11 and ZNF143, and transcriptional coregulators (PubMed:26416877). Involved in control of the cell cycle (PubMed:10629049, PubMed:10779346, PubMed:15190068, PubMed:16624878, PubMed:23629655). Also antagonizes transactivation by ZBTB17 and GABP2; represses ZBTB17 activation of the p15(INK4b) promoter and inhibits its ability to recruit p300 (PubMed:10675337, PubMed:12244100). Coactivator for EGR2 and GABP2 (PubMed:12244100, PubMed:14532282). Tethers the chromatin modifying Set1/Ash2 histone H3 'Lys-4' methyltransferase (H3K4me) and Sin3 histone…

Subunit structure

Composed predominantly of six polypeptides ranging from 110 to 150 kDa and a minor 300 kDa polypeptide (PubMed:10920196). The majority of N- and C-terminal cleavage products remain tightly, albeit non-covalently, associated (PubMed:10920196). Interacts with POU2F1, CREB3, ZBTB17, EGR2, E2F4, CREBZF, SP1, GABP2, Sin3 HDAC complex (SIN3A, HDAC1, HDAC2, SUDS3), SAP30, SIN3B and FHL2…

Subcellular location

Cytoplasm, Nucleus

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4N39X-ray1.76 ÅB=1082-1097
4N3AX-ray1.88 ÅB=1072-1097
5LWVX-ray1.9 ÅA=1078-1095
6MA3X-ray2.0 ÅB=1082-1097
6MA4X-ray2.0 ÅB=1082-1097
6MA5X-ray2.0 ÅB=1082-1097
6MA2X-ray2.1 ÅB=1082-1097
4N3BX-ray2.17 ÅB=1072-1097
4N3CX-ray2.55 ÅB=1072-1097
4GO6X-ray2.7 ÅA/C=360-402, B/D=1806-2035
6MA1X-ray2.75 ÅB=1082-1097

More AlphaFold highlights

About this viewer

MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.