Comparing Pf1N1B4_4296 Histidine transporter, periplasmic histidine-binding protein to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 7 hits to proteins with known functional sites (download)
7yleA Rndmpx in complex with dmsp (see paper)
27% identity, 91% coverage: 31:337/338 of query aligns to 5:297/299 of 7yleA
4xz6A Tmox in complex with tmao (see paper)
26% identity, 88% coverage: 30:325/338 of query aligns to 9:289/291 of 4xz6A
P0AFM2 Glycine betaine/proline betaine-binding periplasmic protein; GBBP from Escherichia coli (strain K12) (see 2 papers)
26% identity, 77% coverage: 72:330/338 of query aligns to 72:327/330 of P0AFM2
Sites not aligning to the query:
1r9qA Structure analysis of prox in complex with proline betaine (see paper)
26% identity, 77% coverage: 72:330/338 of query aligns to 51:306/309 of 1r9qA
Sites not aligning to the query:
3chgA The compatible solute-binding protein opuac from bacillus subtilis in complex with dmsa (see paper)
24% identity, 47% coverage: 179:336/338 of query aligns to 21:160/258 of 3chgA
Sites not aligning to the query:
2b4mA Crystal structure of the binding protein opuac in complex with proline betaine (see paper)
24% identity, 47% coverage: 179:336/338 of query aligns to 27:166/264 of 2b4mA
Sites not aligning to the query:
5nxxC Crystal structure of opuac from b. Subtilis in complex with arsenobetaine (see paper)
24% identity, 47% coverage: 179:336/338 of query aligns to 28:167/265 of 5nxxC
Sites not aligning to the query:
>Pf1N1B4_4296 Histidine transporter, periplasmic histidine-binding protein
MRGFRRLLAATLATFGLLASPVPVFAAQAPIHFADLNWESGSLITDILRIIVEKGYGLPT
DTLPGTTITLETALANNDIQVIGEEWAGRSPVWVKAEAEGKVAALGDTVKGATEGWWVPE
YVIKGDPAKGIKPMAPDLRSISDLPRYKDVFKDPETPGKGRFLNSPIGWTSEVVNKQKLK
AYGLDDSYVNFRSGSGAALDAEISSSIRRGKPVLFYYWSPTPLLGRFKLIQLQEPPFDAE
AWKTLTDADNPNPKPTRSLPSKLSIGVSTPFQKQYPQIAEFFTKVDLPIEALNMALADMS
EKHTPPRQAAEAFMKAHPDVWRAWVPKDVADKVSAALK
Or try a new SitesBLAST search
SitesBLAST's database includes (1) SwissProt entries with experimentally-supported functional features; and (2) protein structures with bound ligands, from the BioLip database.
Lawrence Berkeley National Laboratory