P53261: Pescadillo homolog (NOP7)

Pescadillo homolog (NOP7) is a 605-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P53261.

Gene
NOP7
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Length
605 residues
Mean pLDDT
75.5
Model
AF-P53261-F1 v6
Model created
1 Aug 2025
PDB structures
35

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Model confidence (pLDDT)

The mean pLDDT of this model is 75.5 (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 accurate29%
70 to 90Confident: backbone generally right41%
50 to 70Low: treat with caution14%
Below 50Very low: often disordered regions16%

What pLDDT means and how to read it

Function

Component of the NOP7 complex, which is required for maturation of the 25S and 5.8S ribosomal RNAs and formation of the 60S ribosome

Subunit structure

Component of the NOP7 complex, composed of ERB1, NOP7 and YTM1. The complex is held together by ERB1, which interacts with NOP7 via its N-terminal domain and with YTM1 via a high-affinity interaction between the seven-bladed beta-propeller domains of the 2 proteins. The NOP7 complex associates with the 66S pre-ribosome (PubMed:16287855). Also interacts with NOG1 (PubMed:16888624). May also…

Subcellular location

Nucleus, nucleolus, Nucleus, nucleoplasm

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7UOOEM2.34 Ån=1-605
7V08EM2.36 Ån=1-605
7UQBEM2.43 Ån=1-605
7UQZEM2.44 Ån=1-605
8V83EM2.53 Ån=1-605
8V87EM2.66 Ån=1-605
8V84EM2.7 Ån=1-605
7U0HEM2.76 Ån=1-605
7R6QEM2.98 Ån=1-605
7NACEM3.04 Ån=1-605
7NADEM3.04 Ån=1-110
7R7AEM3.04 Ån=1-605
7R72EM3.07 Ån=1-110
3JCTEM3.08 Ån=1-605
7OHQEM3.1 Ån=1-605
6EM3EM3.2 Ån=1-605
6M62EM3.2 Ån=1-605
7BTBEM3.22 Ån=1-605
6ELZEM3.3 Ån=1-605
7OHXEM3.3 Ån=1-605

Showing 20 of 35 experimental structures (best resolution first).

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