O94851: [F-actin]-monooxygenase MICAL2 (MICAL2)

[F-actin]-monooxygenase MICAL2 (MICAL2) is a 1957-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O94851.

Gene
MICAL2
Organism
Homo sapiens
Length
1957 residues
Mean pLDDT
56.3
Model
AF-O94851-F1 v6
Model created
1 Aug 2025
PDB structures
5

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Model confidence (pLDDT)

The mean pLDDT of this model is 56.3 (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 accurate23%
70 to 90Confident: backbone generally right19%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions54%

What pLDDT means and how to read it

Function

Methionine monooxygenase that promotes depolymerization of F-actin by mediating oxidation of residues 'Met-44' and 'Met-47' on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization (PubMed:24440334, PubMed:29343822). Regulates the disassembly of branched actin networks also by oxidizing ARP3B-containing ARP2/3 complexes leading to ARP3B dissociation from the network (PubMed:34106209). Acts as a key regulator of the SRF signaling pathway elicited by nerve growth factor and serum: mediates oxidation and subsequent depolymerization of nuclear actin, leading to increase MKL1/MRTF-A presence in the nucleus and promote…

Subunit structure

Interacts with PLXNA4 (By similarity). Interacts with RAB1B (PubMed:15694364, PubMed:27552051). Interacts with MAPK1/ERK2 (By similarity). Interacts with RAB35, RAB8A, RAB10, RAB13 and RAB15 (in their GTP-bound forms); binding to RAB35 is of low affinity compared to other Rab proteins; at least in case of RAB8A may bind 2 molecules of RAB8A simultaneously through a high and a low affinity…

Subcellular location

Nucleus, Cytoplasm

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5SZHX-ray2.3 ÅA=1796-1945
5SZJX-ray2.66 ÅB=1796-1945
5SZKX-ray2.8 ÅA=1796-1945
5SZIX-ray2.85 ÅB=1796-1945
2E9KNMRA=516-629

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