P62316: Small nuclear ribonucleoprotein Sm D2 (SNRPD2)

Small nuclear ribonucleoprotein Sm D2 (SNRPD2) is a 118-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P62316.

Gene
SNRPD2
Organism
Homo sapiens
Length
118 residues
Mean pLDDT
90.6
Model
AF-P62316-F1 v6
Model created
1 Aug 2025
PDB structures
80

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Model confidence (pLDDT)

The mean pLDDT of this model is 90.6 (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 accurate78%
70 to 90Confident: backbone generally right16%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions1%

What pLDDT means and how to read it

Function

Plays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome (PubMed:11991638, PubMed:18984161, PubMed:19325628, PubMed:23333303, PubMed:25555158, PubMed:26912367, PubMed:28076346, PubMed:28502770, PubMed:28781166, PubMed:32494006). Component of both the pre-catalytic spliceosome B complex and activated spliceosome C complexes (PubMed:11991638, PubMed:28076346, PubMed:28502770, PubMed:28781166). As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (PubMed:15146077)

Subunit structure

Core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome (PubMed:11991638, PubMed:19325628, PubMed:21516107, PubMed:25555158, PubMed:26912367, PubMed:28076346, PubMed:28502770, PubMed:28781166, PubMed:32494006, PubMed:36797247). Most spliceosomal snRNPs contain a common set of Sm proteins, SNRPB, SNRPD1, SNRPD2,…

Subcellular location

Cytoplasm, cytosol, Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4F7UX-ray1.9 ÅB/D=1-118
1B34X-ray2.5 ÅB=1-118
5XJLX-ray2.5 ÅB=1-118
7EVOEM2.5 Åa=1-118
5XJUX-ray2.58 ÅB=1-118
8H6LEM2.6 Å2c/4c/5c=1-118
8H6KEM2.7 Å2c/4c/5c=1-118
8HK1EM2.7 Åa=1-118
8C6JEM2.8 Åa/m=1-118
6ID1EM2.86 Åd/k=1-118
7DVQEM2.89 Åd/k=1-118
6ID0EM2.9 Åd/k=1-118
5XJTX-ray2.92 ÅB=1-118
6QW6EM2.92 Å42/52=1-118
6ICZEM3.0 Åd/k=1-118
7VPXEM3.0 Åa/i=1-118
8I0REM3.0 Åc/h=1-118
8I0TEM3.0 Åc/h=1-118
8I0VEM3.0 Åc/h=1-118
9GCLEM3.0 Åi=1-118

Showing 20 of 80 experimental structures (best resolution first).

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