Summary
PCMH-like FAD binding
The FAD-binding domains contained in this family fall within the PCMH (p-cresol methyl-hydroxylase) family of FAD binding proteins as defined in [1]. In this family, the structure of the FAD binding domain is comprised of two subdomains. Both of these subdomains have an alpha-beta fold. The first subdomain is comprised of three parallel beta strands, surrounded by alpha helices. The second subdomain contains five antiparallel beta strands, also surrounded by alpha helices. The junction between these two subdomains forms the FAD bind pocket, where the ligand is bound by hydrogen and van der Waals bonds [1].
This clan contains 2 families and the total number of domains in the clan is 84348. The clan was built by RD Finn.
Literature references
- Dym O, Eisenberg D; , Protein Sci 2001;10:1712-1728.: Sequence-structure analysis of FAD-containing proteins. PUBMED:11514662 EPMC:11514662
Members
This clan contains the following 2 member families:
FAD_binding_4 FAD_binding_5External database links
SCOP: | 56176 |
Domain organisation
Below is a listing of the unique domain organisations or architectures from this clan. More...
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Alignments
The table below shows the number of occurrences of each domain throughout the sequence database. More...
Pfam family | Num. domains | Alignment |
---|---|---|
FAD_binding_4 (PF01565) | 68527 (81.2%) | View |
FAD_binding_5 (PF00941) | 15821 (18.8%) | View |
Total: 2 | Total: 84348 | Clan alignment |
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Family relationships
This diagram shows the relationships between members of this clan. More...
Species distribution
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Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the MSD group, to allow us to map Pfam domains onto UniProt three-dimensional structures. The table below shows the mapping between the Pfam families in this clan, the corresponding UniProt entries, and the region of the three-dimensional structures that are available for that sequence.
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