DAP Structural Analysis

Chain Sequence of 2ijz-A

>gi|119390187|pdb|2IJZ|A Chain A, Crystal Structure Of Aminopeptidase RAELNQGLIDFLKASPTPFHATASLARRLEAAGYRRLDERDAWHTETGGRYYVTRNDSSLIAIRLGRRSP LESGFRLVGAHTDSPCLRVKPNPEIARNGFLQLGVEVYGGALFAPWFDRDLSLAGRVTFRANGKLESRLV DFRKAIAVIPNLNIHLNRAANEGWPINAQNELPPIIAQLAPGEAADFRLLLDEQLLREHGITADVVLDYE LSFYDTQSAAVVGLNDEFIAGARLDNLLSCHAGLEALLNAEGDENCILVCTDHEEVGSCSHCGADGPFLE QVLRRLLPEGDAFSRAIQRSLLVSADNAHGVHPNYADRHDANHGPALNGGPVIKINSNQRYATNSETAGF FRHLCQDSEVPVQSFVTRSDMGCGSTIGPITASQVGVRTVDIGLPTFAMHSIRELAGSHDLAHLVKVLGA FYASSELP

Structure of 2ijz-A chain

Fig x: PDBsum Analysis of the secondary protein sequence giving rise to how the protein folds in the motifs of turns and hairpins.

Fig x: Topology of 2ijz-A chain giving a simplified understanding of how the protein folds.

Structural Analysis of 2ijz-A chain

Fig x: A) Front view of 2ijz-A chain structure; B) Back view of 2ijz-A –chain Structure; Pictures showing the loops (pink), beta-sheet (magenta) and alpha helix (greenish blue) of the structure taken from PyMOL.

Fig X: Part of DALI search results gathering structurally related proteins. The three marked proteins in orange were structurally aligned using PyMOL. Proteins 13 to 18 were not taken as no scientific evidence of the protein has been obtained yet.

From here, the results of the conserved regions in the sequence is taken from the evolutionary analysis part. These conserved regions are then marked out in red in the following image below (Fig:X).

Positions of conserved regions

Fig X: Structure of 2ijz-A with conserved regions colored in red.

Structural Comparison of 2ijz-A and Respective Proteins

Comparison of 2ijz-A chain (yellow) and 1vhe-A chain (blue) and both of the similar conserved regions are marked in red.

Comparison of 2ijz-A chain (yellow) and 1xfo-A chain (blue) and both of the similar conserved regions are marked in red.