Q0JRZ9: F-BAR domain only protein 2 (FCHO2)

F-BAR domain only protein 2 (FCHO2) is a 810-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q0JRZ9.

Gene
FCHO2
Organism
Homo sapiens
Length
810 residues
Mean pLDDT
76.2
Model
AF-Q0JRZ9-F1 v6
Model created
1 Aug 2025
PDB structures
7

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Model confidence (pLDDT)

The mean pLDDT of this model is 76.2 (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 accurate59%
70 to 90Confident: backbone generally right8%
50 to 70Low: treat with caution3%
Below 50Very low: often disordered regions30%

What pLDDT means and how to read it

Function

Functions in an early step of clathrin-mediated endocytosis. Has both a membrane binding/bending activity and the ability to recruit proteins essential to the formation of functional clathrin-coated pits. Has a lipid-binding activity with a preference for membranes enriched in phosphatidylserine and phosphoinositides (Pi(4,5) biphosphate) like the plasma membrane. Its membrane-bending activity might be important for the subsequent action of clathrin and adaptors in the formation of clathrin-coated vesicles. Involved in adaptor protein complex AP-2-dependent endocytosis of the transferrin receptor, it also functions in the AP-2-independent endocytosis of the LDL receptor

Subunit structure

Homodimer; disulfide-linked. May form homotetramer. Interacts with AP2A1. Interacts with EPS15, EPS15R, ITSN1 and ITSN2; recruit those scaffolding proteins which in turn may interact with the adaptor protein complex AP-2 at the plasma membrane. Interacts with DAB2 (via DPF motifs); mediates LDL receptor/LDLR endocytosis

Subcellular location

Membrane, clathrin-coated pit

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7OITX-ray1.65 ÅBBB=422-432
7OIQX-ray1.85 ÅCCC/DDD=422-432
7OHZX-ray2.27 ÅA/B=316-351
2V0OX-ray2.3 ÅA/B/C=3-274
7OI5X-ray2.61 ÅB/D=316-351
7OHOX-ray2.88 ÅBBB=358-444
7OG1X-ray3.25 ÅDDD/GGG=314-444

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