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Paper Details

Structure of the first representative of Pfam family PF04016 (DUF364) reveals enolase and Rossmann-like folds that combine to form a unique active site with a possible role in heavy-metal chelation.
Acta Crystallogr Sect F Struct Biol Cryst Commun
2
2010
DUF364, Desulfitobacterium hafniense DCB-2, Dhaf4260, Pfam, Rossmann-like methyltransferases, active site, enolase, enolase N-, enolase-like fold, flavins, pterins

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