# Proteo3Dnet

Integrating 3D structure information to proteomics data

Integrating 3D structure information to proteomics data

The results of the search for protein-protein interactions is summarized using several tables:

**The homology_detection table summarizes the results of the homology search.**

**A second table summarizes the results of the search for protein hetero-complexes**.

The table columns describe, from left to right: the complex unique identifier, the maximal average sequence identity of chain with the corresponding protein of the input data over all equivalent template complexes of known structure identified, the number of input proteins mapped to the complex structure, the number of PDB structures corresponding to similar complexes, the maximum completeness of the input/template alignment, the number of chains of the template complex that do not have an identified equivalent in the input data, the parent and child complex identifiers for entries corresponding to smaller complexes. For instance, for c001, one observes that 4 over 8 chains seem not to have an equivalent in the input data. One also sees that c002 (3 chains) seems to correspond to an assembly encompassing that of c004 (2 chains). Clicking on the complex unique identifier gives access to an ancillary table describing the mapping between the complex structures and the input proteins. For instance, clicking on the complex c002, the table describes the input mapping to all chains of all 25 structures identified with the same assembly, belonging to different species. Interestingly, one sees that better sequence identity seems to occur for structures resolved for the RAT (98.7%), and not for H. Sapiens (95.3%). Looking in more detail, one observes that this difference comes in fact from AAPK1 (86%), as the human structure contains the AAPK2 paralog instead of AAPK1.

**A third table summarizes the results of the homo-oligomeric state of each protein**.