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Figure 4 | Orphanet Journal of Rare Diseases

Figure 4

From: Novel C16orf57 mutations in patients with Poikiloderma with Neutropenia: bioinformatic analysis of the protein and predicted effects of all reported mutations

Figure 4

Structural model of C16orf57 protein. A) Predicted 2H phosphoesterase family fold of human C16orf57, built by MODELLER [20] from the 1VGJ template structure (HHpred match probability of 99.9, E-value 2.9×10-29). Cartoon form with the chain colour-ramped from N-terminal residue 80 (dark blue) to C-terminal residue 265 (red); β-strands are labelled A-H and α-helices numbered 1-4. B) The two α+β lobes form an active site groove marked by the signature 2H motifs. Side chains are shown for the catalytic H120xS122 and H208xS210 residues. The flattened chain topology of human C16orf57 shows the structural repeats (boxed) and active site motifs that characterize the 2H phosphoesterase fold family. Identical labels and colours are drawn from the structural model in A and B.

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