pLDDT
The pLDDT value is assigned to each individual residue and stored in coordinate files instead of temperature factors. Different from temperature factors, high values indicate high confidence in atomic positions, and low values low confidence (scale of 0 to 100). This value is named pLDDT because it predicts the so-called LDDT value (Local Distance Difference Test, [1]), a way to characterize the difference of two related conformations without aligning the structures.
Expected distance error
Alphafold also predicts the expected error in the distance of two residues. Thus, this is a 2-dimensional (pairwise) data set. The plot of the data is shown below. On the right, you can see the mapped by color on the second residue. If you hover over the residue, it will show the estimated distance error. It becomes apparent that the distance between residue 1000 and residues in the N-terminal part of the protein are ill-defined. However, if you show the expected errors to residue 400 (by using the links below), the N-terminal domain is well-defined in isolation. It is the relative domain orientation that is not well predicted. If you explore some other of the residues provided below, you will discover that there are subdomains within the N-terminal as well as the C-terminal domain. This is experimentally supported, e.g. for the cap subdomain (click on 680 below) that plays a role in protecting B12 from unwanted redox reactions.
Residue
Residues near the apparent domain interface
Some residues that are highlighted in the are near the apparent domain interface. This might be because they have spatial neighbors in a different domain whose relative orientation is ill-defined. Thus, it would be a misinterpretation to conclude that these residues are disordered with respect to their own domain. The LDDT algorithm was choosen to suppress these inter-domain signals (by choosing a small radius of neighbors considered), but there does seem to be some overlap of intra-domain disorder and inter-domain orientation within the pLDDT measure.
Other examples of model uncertainty
The prediction of the UvrB structure [1] shows some off-diagonal elements in the 2D distance uncertainty plot. This is because domains are not consecutive in the sequence; instead, along the sequence, domain 1 is "interrupted" by domain 2 (spanning residues 150-250, approximately). In addition, the very C-terminal part of the protein is structured but attached to the remainder of the protein by just a flexible tether. These features are apparent in the 2D distance plot, but it would be nice to visualize them by mapping them on the 3D structure.
The prediction of the bovine actin structure shows high certainty of most elements, and no indication of domain movements. Instead, there is one loop that has low scores in the 1D and 2D certainty data. In this simpler case, mapping the 1D certainty data on the 3D structure gives sufficient information.
