Q9BQ90: Kelch domain-containing protein 3 (KLHDC3)

Kelch domain-containing protein 3 (KLHDC3) is a 382-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9BQ90.

Gene
KLHDC3
Organism
Homo sapiens
Length
382 residues
Mean pLDDT
94.1
Model
AF-Q9BQ90-F1 v6
Model created
1 Aug 2025
PDB structures
3

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Model confidence (pLDDT)

The mean pLDDT of this model is 94.1 (very high 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 accurate87%
70 to 90Confident: backbone generally right9%
50 to 70Low: treat with caution3%
Below 50Very low: often disordered regions1%

What pLDDT means and how to read it

Function

Substrate-recognition component of a Cul2-RING (CRL2) E3 ubiquitin-protein ligase complex of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation (PubMed:29775578, PubMed:29779948). The C-degron recognized by the DesCEND pathway is usually a motif of less than ten residues and can be present in full-length proteins, truncated proteins or proteolytically cleaved forms (PubMed:29775578, PubMed:29779948). The CRL2(KLHDC3) complex specifically recognizes proteins with a glycine (Gly) at the C-terminus, leading to their ubiquitination and degradation: recognizes the…

Subunit structure

Component of a CRL2(KLHDC3) complex, also named ECS(KLHDC3) complex, composed of CUL2, Elongin BC (ELOB and ELOC), RBX1 and substrate-specific adapter KLHDC3 (PubMed:29775578, PubMed:29779948). May form oligomers as a KLHDC3-ELOB-ELOC complex; this interaction is likely autoinhibitory for the E3 ligase complex (PubMed:36805027)

Subcellular location

Cytoplasm

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
9D1ZX-ray1.88 ÅA=1-382
9D1IX-ray2.0 ÅA=1-382
9D1YX-ray2.6 ÅA=1-382

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