Q6TQR6: RNA-directed RNA polymerase L (L)

RNA-directed RNA polymerase L (L) is a 734-residue protein from Crimean-Congo hemorrhagic fever virus. This is its AlphaFold structure prediction, created 3 Jul 2025. UniProt accession: Q6TQR6.

Gene
L
Organism
Crimean-Congo hemorrhagic fever virus
Length
734 residues
Mean pLDDT
69.0
Model
AF-0000000365774956 v1
Model created
3 Jul 2025
PDB structures
20

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Model confidence (pLDDT)

The mean pLDDT of this model is 69.0 (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 accurate13%
70 to 90Confident: backbone generally right39%
50 to 70Low: treat with caution31%
Below 50Very low: often disordered regions17%

What pLDDT means and how to read it

Function

Displays RNA-directed RNA polymerase, deubiquitinating and deISGylase activities (PubMed:18078692, PubMed:21228232, PubMed:21245344, PubMed:23345508). RNA-dependent RNA polymerase is responsible for replication and transcription of the viral RNA genome (PubMed:18078692). During transcription, synthesizes subgenomic RNAs and assures their capping by a cap-snatching mechanism, which involves the endonuclease activity cleaving the host capped pre-mRNAs (By similarity). These short capped RNAs are then used as primers for viral transcription (By similarity). The deubiquitinating and deISGylating activities specifically cleaves poly-ubiquitinated conjugates and ISG15 from RIG-I, interfering…

Subunit structure

Interacts (via N-terminus) with host ISG15 (via C-terminus); the deISGylase activity of the viral protein interferes with antiviral signaling pathways mediated by NF-kappaB and IRF signalings (PubMed:21245344, PubMed:21266548). Interacts with host ubiquitin (PubMed:21245344)

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5V5HX-ray1.5 ÅA=1-169
3PHXX-ray1.6 ÅA=1-183
3PRPX-ray1.7 ÅA/C=1-170
3PHWX-ray2.0 ÅA/C/E/G=1-183
5V5GX-ray2.1 ÅA/C=1-183
3PHUX-ray2.2 ÅA/B=1-217
5V5IX-ray2.2 ÅA/C=1-169
3PRMX-ray2.3 ÅA/C=1-170
3PSEX-ray2.3 ÅA=1-169
3ZNHX-ray2.3 ÅA=1-183
3PT2X-ray2.5 ÅA=1-184
9YBNEM2.53 ÅA=1-3945
9YBMEM2.62 ÅA=1-3945
9XD5EM2.72 ÅA=1-3945
9XD6EM2.74 ÅA=1-3945
9XD4EM2.79 ÅA=1-3945
9XE9EM2.81 ÅA=1-3945
9XECEM2.98 ÅA=1-3945
9XE7EM3.02 ÅA=1-3945
9XE6EM3.09 ÅA=1-3945

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