Figure 4.

The 3D-interologs database search results of using human NXT1 (UniProt accession number Q9UKK6) as query. (A) Eight interacting partners of NXT1 are found in the 3D-Interologs. For each interacting partner, this server provides UniProt accession number, protein description, organism and Gene Ontology annotation. (B) Detailed interactions between the query and its interacting partner (UniProt accession number Q9UBU9) are indicated via the structure template which consists of NXT1 (PDB entry 1jkg-A) and NXF1 (PDB entry 1jkg-B). The contact residues of NXT1 (query side) and NXF1 (partner side) are colored by red and blue, respectively. The contact residues forming hydrogen bonds (green and dash) are given the atom details. (C) The interacting evolution analysis by using multiple sequence alignments of hit interacting partners of the query across multiple species. The 3D- interologs yields 10 interologs of the query template structure. The contacted residues are marked in template structure based on their interacting characteristics, including hydrogen-bond residues (green); conserved residues (orange); both (yellow), and others (gray). The couple-conserved contact positions are colored in the multiple alignments according to the physical-chemical property of amino acid residues. Twenty amino acid types are classified into 7 groups, namely polar positive (His,Arg, and Lys, blue); polar negative (Asp and Glu, red); polar neutral (Ser, Thr, Asn and Gln, green); cystein (yellow); non-polar aliphatic (Ala, Val, Leu, Ile and Met, gray); non-polar aromatic (Phe, Tyr and Trp, pink); and others: (Gly and Pro, brown).

Lo et al. BMC Genomics 2010 11(Suppl 3):S7   doi:10.1186/1471-2164-11-S3-S7