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Paper Details

The structure of SSO2064, the first representative of Pfam family PF01796, reveals a novel two-domain zinc-ribbon OB-fold architecture with a potential acyl-CoA-binding role.
Acta Crystallogr Sect F Struct Biol Cryst Commun
17
2010
C, CoA, DUF35, DUF35 family, N, Pfam, SSO2064, acyl-CoA, acyl-CoA-binding proteins, fatty-acid, rubredoxin, rubredoxin-like, zinc

Datasets

Dataset
Description
Source Link
PfamA database of conserved protein families and domains. Pfam is a member database of InterPro.Link
PfamMultiple sequence alignments and hidden Markov models of common protein domainsLink
PfamMultiple sequence alignments and hidden Markov models of common protein domainsLink
PfamA database of conserved protein families and domains. Pfam is a member database of InterPro.Link
PfamA database of conserved protein families and domains. Pfam is a member database of InterPro.Link
PfamMultiple sequence alignments and hidden Markov models of common protein domainsLink
PfamA database of conserved protein families and domains. Pfam is a member database of InterPro.Link
PfamA database of conserved protein families and domains. Pfam is a member database of InterPro.Link
PfamA database of conserved protein families and domains. Pfam is a member database of InterPro.Link
PfamMultiple sequence alignments and hidden Markov models of common protein domainsLink
PfamMultiple sequence alignments and hidden Markov models of common protein domainsLink
PfamMultiple sequence alignments and hidden Markov models of common protein domainsLink
PfamA database of conserved protein families and domains. Pfam is a member database of InterPro.Link
PfamA database of conserved protein families and domains. Pfam is a member database of InterPro.Link
PfamA database of conserved protein families and domains. Pfam is a member database of InterPro.Link
Release 1.2