Q8NB78: Lysine-specific histone demethylase 2 (KDM1B)

Lysine-specific histone demethylase 2 (KDM1B) is a 822-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q8NB78.

Gene
KDM1B
Organism
Homo sapiens
Length
822 residues
Mean pLDDT
91.3
Model
AF-Q8NB78-F1 v6
Model created
1 Aug 2025
PDB structures
15

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Model confidence (pLDDT)

The mean pLDDT of this model is 91.3 (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 right2%
50 to 70Low: treat with caution2%
Below 50Very low: often disordered regions8%

What pLDDT means and how to read it

Function

Histone demethylase that demethylates 'Lys-4' of histone H3, a specific tag for epigenetic transcriptional activation, thereby acting as a corepressor. Required for de novo DNA methylation of a subset of imprinted genes during oogenesis. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Demethylates both mono- and di-methylated 'Lys-4' of histone H3. Has no effect on tri-methylated 'Lys-4', mono-, di- or tri-methylated 'Lys-9', mono-, di- or tri-methylated 'Lys-27', mono-, di- or tri-methylated 'Lys-36' of histone H3, or on mono-, di- or tri-methylated 'Lys-20' of histone H4. Alone, it is unable to demethylate H3K4me on nucleosomes…

Subunit structure

Interacts with its cofactor GLYR1 at nucleosomes; this interaction stimulates H3K4me1 and H3K4me2 demethylation (PubMed:23260659, PubMed:30970244). In contrast to KDM1A, does not form a complex with RCOR1/CoREST (Probable). Possible accessory component of the polycomb repressive deubiquitinase (PR-DUB) complex, at least composed of BAP1, one of ASXL1, ASXL2 or (probably) ASXL3 and one of MBD5 or…

Subcellular location

Nucleus, Chromosome

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4HSUX-ray1.99 ÅA=51-822
4GUTX-ray2.0 ÅA=51-822
7XE2X-ray2.05 ÅA/B=30-822
7XE1X-ray2.07 ÅA/B=30-822
4FWEX-ray2.13 ÅA=30-822
4GUSX-ray2.23 ÅA=51-822
4GUUX-ray2.3 ÅA=51-822
4GURX-ray2.51 ÅA=51-822
4FWFX-ray2.7 ÅA=30-822
7XE3X-ray2.82 ÅA/B=30-822
4FWJX-ray2.9 ÅA/B=30-822
4GU1X-ray2.94 ÅA/B=51-822
4GU0X-ray3.1 ÅA/B/C/D=51-822
6R1UEM4.36 ÅK=51-822
6R25EM4.61 ÅK=51-822

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