P38632: E3 SUMO-protein ligase MMS21 (MMS21)

E3 SUMO-protein ligase MMS21 (MMS21) is a 267-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P38632.

Gene
MMS21
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Length
267 residues
Mean pLDDT
86.4
Model
AF-P38632-F1 v6
Model created
1 Aug 2025
PDB structures
11

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Model confidence (pLDDT)

The mean pLDDT of this model is 86.4 (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 accurate60%
70 to 90Confident: backbone generally right25%
50 to 70Low: treat with caution12%
Below 50Very low: often disordered regions2%

What pLDDT means and how to read it

Function

Acts as an E3 ligase mediating SUMO/Smt3 attachment to SMC5 and YKU70. Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks

Subunit structure

Component of the Smc5-Smc6 complex which consists of KRE29, NSE1, NSE2/MMS21, NSE3, NSE4, NSE5, SMC5 and SMC6

Subcellular location

Nucleus, Cytoplasm

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3HTKX-ray2.31 ÅC=1-267
7P47X-ray3.31 ÅA=27-267
7YQHEM5.6 ÅC=1-267
8I4VEM5.97 ÅC=4-254
8I21EM6.02 ÅC=1-267
8WJOEM6.04 ÅC=1-267
8WJLEM6.15 ÅC=1-267
7YLMEM6.17 ÅC=1-267
8I4UEM6.73 ÅC=1-267
7QCDEM8.0 ÅC=2-267
8I4XEM8.5 ÅC=1-267

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