O75496: Geminin (GMNN)

Geminin (GMNN) is a 209-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O75496.

Gene
GMNN
Organism
Homo sapiens
Length
209 residues
Mean pLDDT
69.5
Model
AF-O75496-F1 v6
Model created
1 Aug 2025
PDB structures
6

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Model confidence (pLDDT)

The mean pLDDT of this model is 69.5 (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 accurate28%
70 to 90Confident: backbone generally right14%
50 to 70Low: treat with caution40%
Below 50Very low: often disordered regions18%

What pLDDT means and how to read it

Function

Inhibits DNA replication by preventing the incorporation of MCM complex into pre-replication complex (pre-RC) (PubMed:14993212, PubMed:20129055, PubMed:24064211, PubMed:9635433). It is degraded during the mitotic phase of the cell cycle (PubMed:14993212, PubMed:24064211, PubMed:9635433). Its destruction at the metaphase-anaphase transition permits replication in the succeeding cell cycle (PubMed:14993212, PubMed:24064211, PubMed:9635433). Inhibits histone acetyltransferase activity of KAT7/HBO1 in a CDT1-dependent manner, inhibiting histone H4 acetylation and DNA replication licensing (PubMed:20129055). Inhibits the transcriptional activity of a subset of Hox proteins, enrolling them in…

Subunit structure

Homotetramer (PubMed:15260975, PubMed:15313623, PubMed:15378034, PubMed:19906994). Interacts with CDT1; this inhibits binding of the MCM complex to origins of replication (PubMed:14993212, PubMed:15260975, PubMed:19906994, PubMed:21543332). The complex with CDT1 exists in two forms, a 'permissive' heterotrimer and an 'inhibitory' heterohexamer (PubMed:14993212, PubMed:15260975, PubMed:19906994).…

Subcellular location

Cytoplasm, Nucleus

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
1T6FX-ray1.47 ÅA/B=109-145
1UIIX-ray2.0 ÅA/B=70-152
4BRYX-ray2.89 ÅA=83-160
2WVRX-ray3.3 ÅA/B=1-209
7KLZX-ray3.4 ÅC/D=195-209
2LP0NMRB=171-190

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