O75367: Core histone macro-H2A.1 (MACROH2A1)

Core histone macro-H2A.1 (MACROH2A1) is a 369-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O75367.

Gene
MACROH2A1
Organism
Homo sapiens
Length
369 residues
Mean pLDDT
82.9
Model
AF-O75367-F1 v6
Model created
1 Aug 2025
PDB structures
13

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Model confidence (pLDDT)

The mean pLDDT of this model is 82.9 (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 accurate68%
70 to 90Confident: backbone generally right10%
50 to 70Low: treat with caution4%
Below 50Very low: often disordered regions18%

What pLDDT means and how to read it

Function

Variant histone H2A which replaces conventional H2A in a subset of nucleosomes where it represses transcription (PubMed:12718888, PubMed:15621527, PubMed:16428466). Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template (PubMed:15897469). Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability (PubMed:15897469). DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Involved in stable X chromosome inactivation (PubMed:15897469). Inhibits the binding of…

Subunit structure

The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. Interacts with HDAC1 and HDAC2 (PubMed:16107708). Interacts with SPOP (PubMed:15897469, PubMed:19818708). Part of a complex consisting of MACROH2A1, CUL3 and SPOP (PubMed:15897469, PubMed:19818708)

Subcellular location

Nucleus, Chromosome

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3HSVX-ray1.43 ÅM=171-186
1ZR3X-ray1.66 ÅA/B/C/D=162-369
3IVBX-ray1.75 ÅM=167-181
3IIDX-ray1.9 ÅA=162-369
3IIFX-ray2.1 ÅA/B/C=162-369
5IITX-ray2.13 ÅA/B/C/D=181-366
3HQHX-ray2.3 ÅM=167-181
2FXKX-ray2.54 ÅA/B=162-369
2F8NX-ray2.9 ÅG=1-120
1ZR5X-ray2.92 ÅA/B=161-369
1U35X-ray3.0 ÅC/G=1-120
7D3YX-ray3.11 ÅA/B=181-369
5LNCX-ray3.29 ÅA/B=182-366

More AlphaFold highlights

About this viewer

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