P19388: DNA-directed RNA polymerases I, II, and III subunit RPABC1 (POLR2E)

DNA-directed RNA polymerases I, II, and III subunit RPABC1 (POLR2E) is a 210-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P19388.

Gene
POLR2E
Organism
Homo sapiens
Length
210 residues
Mean pLDDT
93.1
Model
AF-P19388-F1 v6
Model created
1 Aug 2025
PDB structures
57

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Model confidence (pLDDT)

The mean pLDDT of this model is 93.1 (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 accurate89%
70 to 90Confident: backbone generally right11%
50 to 70Low: treat with caution1%
Below 50Very low: often disordered regions0%

What pLDDT means and how to read it

Function

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. Pols are composed of mobile elements that move relative to each other. In Pol II, POLR2E/RPABC1 is part of the lower jaw surrounding the central large cleft and thought to grab the incoming DNA template

Subunit structure

Component of the RNA polymerase I (Pol I), RNA polymerase II (Pol II) and RNA polymerase III (Pol III) complexes consisting of at least 13, 12 and 17 subunits, respectively (PubMed:16809778, PubMed:33335104, PubMed:33558764, PubMed:33558766, PubMed:33674783, PubMed:34675218, PubMed:9852112). Pol I complex consists of a ten-subunit catalytic core composed of POLR1A/RPA1, POLR1B/RPA2,…

Subcellular location

Nucleus, Nucleus, nucleolus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
9EHZEM2.6 ÅE=1-210
7OB9EM2.7 ÅE=1-210
8XSOEM2.7 ÅE=1-210
7AE1EM2.8 ÅE=1-210
9K39EM2.8 ÅE=1-210
7VBBEM2.81 ÅE=1-210
7VBAEM2.89 ÅE=1-210
7D58EM2.9 ÅE=1-210
9K36EM2.9 ÅE=1-210
9K2GEM3.0 ÅE=1-210
9K3UEM3.0 ÅE=1-210
7VBCEM3.01 ÅE=1-210
7AE3EM3.1 ÅE=1-210
7D59EM3.1 ÅE=1-210
7OBAEM3.1 ÅE=1-210
9K38EM3.1 ÅE=1-210
8XRMEM3.13 ÅE=1-210
9EI1EM3.2 ÅE=1-210
9EI3EM3.2 ÅE=1-210
9FSOEM3.28 ÅM=1-210

Showing 20 of 57 experimental structures (best resolution first).

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