O75643: U5 small nuclear ribonucleoprotein 200 kDa helicase (SNRNP200)

U5 small nuclear ribonucleoprotein 200 kDa helicase (SNRNP200) is a 2136-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O75643.

Gene
SNRNP200
Organism
Homo sapiens
Length
2136 residues
Mean pLDDT
82.8
Model
AF-O75643-F1 v6
Model created
1 Aug 2025
PDB structures
79

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Model confidence (pLDDT)

The mean pLDDT of this model is 82.8 (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 accurate46%
70 to 90Confident: backbone generally right42%
50 to 70Low: treat with caution3%
Below 50Very low: often disordered regions10%

What pLDDT means and how to read it

Function

Catalyzes the ATP-dependent unwinding of U4/U6 RNA duplices, an essential step in the assembly of a catalytically active spliceosome (PubMed:35241646). Plays a role in pre-mRNA splicing as a core component of precatalytic, catalytic and postcatalytic spliceosomal complexes (PubMed:28502770, PubMed:28781166, PubMed:29301961, PubMed:29360106, PubMed:29361316, PubMed:30315277, PubMed:30705154, PubMed:30728453). As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). Involved in spliceosome assembly, activation and disassembly. Mediates changes in the dynamic network of RNA-RNA interactions in the spliceosome

Subunit structure

Component of a core complex containing at least PRPF8, SNRNP200, EFTUD2 and SNRNP40. Component of the U5 snRNP and U4/U6-U5 tri-snRNP complexes, building blocks of the spliceosome. Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39…

Subcellular location

Nucleus

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
2Q0ZX-ray2.0 ÅX=1808-2136
8BCEX-ray2.05 ÅB=394-2136
8BC9X-ray2.3 ÅB=394-2136
8BCCX-ray2.35 ÅB=394-2136
8BCBX-ray2.38 ÅB=394-2136
6S8QX-ray2.39 ÅB=394-2136
8BC8X-ray2.39 ÅB=394-2136
8BCGX-ray2.39 ÅB=394-2136
8BCFX-ray2.42 ÅB=394-2136
7BDKX-ray2.52 ÅB=394-2136
7BDJX-ray2.59 ÅB=394-2136
6S9IX-ray2.6 ÅB=394-2136
8H6LEM2.6 Å5D=1-2136
4F92X-ray2.66 ÅB=402-2125
7BDLX-ray2.69 ÅB=394-2136
4F91X-ray2.7 ÅB=402-2125
8H6KEM2.7 Å5D=1-2136
5URJX-ray2.75 ÅA=395-2129
7OS2EM2.76 ÅB=395-2129
5URMX-ray2.8 ÅA/B=395-2129

Showing 20 of 79 experimental structures (best resolution first).

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