Q8NHM5: Lysine-specific demethylase 2B (KDM2B)

Lysine-specific demethylase 2B (KDM2B) is a 1336-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q8NHM5.

Gene
KDM2B
Organism
Homo sapiens
Length
1336 residues
Mean pLDDT
67.8
Model
AF-Q8NHM5-F1 v6
Model created
1 Aug 2025
PDB structures
4

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Model confidence (pLDDT)

The mean pLDDT of this model is 67.8 (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 accurate38%
70 to 90Confident: backbone generally right19%
50 to 70Low: treat with caution4%
Below 50Very low: often disordered regions39%

What pLDDT means and how to read it

Function

Histone demethylase that demethylates 'Lys-4' and 'Lys-36' of histone H3, thereby playing a central role in histone code (PubMed:16362057, PubMed:17994099, PubMed:26237645). Preferentially demethylates trimethylated H3 'Lys-4' and dimethylated H3 'Lys-36' residue while it has weak or no activity for mono- and tri-methylated H3 'Lys-36' (PubMed:16362057, PubMed:17994099, PubMed:26237645). Preferentially binds the transcribed region of ribosomal RNA and represses the transcription of ribosomal RNA genes which inhibits cell growth and proliferation (PubMed:16362057, PubMed:17994099). May also serve as a substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin…

Subunit structure

Interacts with SKP1, forming heterodimers (PubMed:27568929). The heterodimeric KDM2B-SKP1 complex interacts with the PCGF1-BCORL1 heterodimeric complex to form a homotetrameric polycomb repression complex 1 (PRC1.1) (PubMed:27568929). Directly interacts with CUL1. The SKP1-KDM2B complex interacts with UBB (PubMed:30033217)

Subcellular location

Nucleus, nucleolus, Nucleus, Chromosome

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4O64X-ray2.13 ÅA/B/C=607-723
8HCUX-ray2.2 ÅA=1103-1336
5JH5X-ray2.55 ÅA=1059-1336
6BVAX-ray2.66 ÅE/F=1060-1104

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