Q5SW96: Low density lipoprotein receptor adapter protein 1 (LDLRAP1)

Low density lipoprotein receptor adapter protein 1 (LDLRAP1) is a 308-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q5SW96.

Gene
LDLRAP1
Organism
Homo sapiens
Length
308 residues
Mean pLDDT
69.4
Model
AF-Q5SW96-F1 v6
Model created
1 Aug 2025
PDB structures
1

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Model confidence (pLDDT)

The mean pLDDT of this model is 69.4 (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 accurate39%
70 to 90Confident: backbone generally right11%
50 to 70Low: treat with caution15%
Below 50Very low: often disordered regions36%

What pLDDT means and how to read it

Function

Adapter protein (clathrin-associated sorting protein (CLASP)) required for efficient endocytosis of the LDL receptor (LDLR) in polarized cells such as hepatocytes and lymphocytes, but not in non-polarized cells (fibroblasts). May be required for LDL binding and internalization but not for receptor clustering in coated pits. May facilitate the endocytosis of LDLR and LDLR-LDL complexes from coated pits by stabilizing the interaction between the receptor and the structural components of the pits. May also be involved in the internalization of other LDLR family members. Binds to phosphoinositides, which regulate clathrin bud assembly at the cell surface. Required for trafficking of LRP2 to…

Subunit structure

Interacts (via PID domain) with LDLR (via NPXY motif) (PubMed:12221107). Binds to soluble clathrin trimers (PubMed:12221107). Interacts with AP2B1; the interaction mediates the association with the AP-2 complex (PubMed:12221107). Interacts with VLDLR (By similarity). Interacts with LRP2 (By similarity)

Subcellular location

Cytoplasm

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
2G30X-ray1.6 ÅP=252-267

More AlphaFold highlights

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