P52756: RNA-binding protein 5 (RBM5)

RNA-binding protein 5 (RBM5) is a 815-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P52756.

Gene
RBM5
Organism
Homo sapiens
Length
815 residues
Mean pLDDT
62.4
Model
AF-P52756-F1 v6
Model created
1 Aug 2025
PDB structures
10

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Model confidence (pLDDT)

The mean pLDDT of this model is 62.4 (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 accurate7%
70 to 90Confident: backbone generally right39%
50 to 70Low: treat with caution13%
Below 50Very low: often disordered regions41%

What pLDDT means and how to read it

Function

Component of the spliceosome A complex. Binds to ssRNA containing the consensus sequence 5'-AGGUAA-3' (PubMed:21256132). Regulates alternative splicing of a number of mRNAs. May modulate splice site pairing after recruitment of the U1 and U2 snRNPs to the 5' and 3' splice sites of the intron. May both positively and negatively regulate apoptosis by regulating the alternative splicing of several genes involved in this process, including FAS and CASP2/caspase-2. In the case of FAS, promotes exclusion of exon 6 thereby producing a soluble form of FAS that inhibits apoptosis. In the case of CASP2/caspase-2, promotes exclusion of exon 9 thereby producing a catalytically active form of…

Subunit structure

Component of the spliceosome A complex (also known as the prespliceosome). Appears to dissociate from the spliceosome upon formation of the spliceosome B complex (also known as the precatalytic spliceosome), in which the heterotrimeric U4/U6.U5 snRNPs are bound. Interacts with U2AF2; this interaction is direct. Also interacts with ACIN1, PRPF8, SFRS3, SNRPB, SNRPN, SNRNP70 and SNRNP200; these…

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7PCVX-ray2.42 ÅA/B=94-210
9ZE2EM3.26 ÅA=1-815
7PDVX-ray3.49 ÅA/C/E/G=94-210
9ZECEM3.61 ÅA=1-815
9ZEDEM3.94 ÅA=1-815
2LK0NMRA=181-210
2LK1NMRA=181-210
2LKZNMRA=231-316
5MF9NMRA=451-511
5MFYNMRA=451-511

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