 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 4]](hv5080fig4mag.jpg)
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Figure 4
Alignment of AMPK γ1 (UniProt entry P54619; CBS3+4, amino acids 182–323; CBS1+2, amino acids 42–177), SNF4 (Saccharomyces cerevisiae, UniProt entry P12904; CBS3+4, amino acids 187–318; CBS1+2, amino acids 35–175), human IMPDH II (UniProt entry P12268, amino acids 112–232), bacterial IMPDH (PDB code 1zfj , UniProt entry Q8K5G1, amino acids 95–211), CBS (UniProt entry P35520, amino acids 416–543) and CLC-0 (Torpedo marmorata, GenBank X56758, amino acids 536–606 and 718–769, break in sequence indicated by *). Residues involved in interactions with AMP in AMPK γ1 CBS3+4 are in underlined in bold. Residue 444 of CBS, which is substituted by asparagine in homocysteineurea, is shown in underlined italics. The GhxS/TxS/TD motif is in bold. Secondary-structural elements derived from the AMPK γ1 (182–325) structure (above) and CLC-0 structure (below) are shown. |
![[Figure 4]](hv5080fig4.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
