1ixg

PHOSPHATE-BINDING PROTEIN MUTANT WITH THR 141 REPLACED BY ASP (T141D), COMPLEXED WITH PHOSPATEPHOSPHATE-BINDING PROTEIN MUTANT WITH THR 141 REPLACED BY ASP (T141D), COMPLEXED WITH PHOSPATE

Structural highlights

1ixg is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	PHO-S (Escherichia coli)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

A very short hydrogen bond between an Asp and a phosphate is established in two high resolution structures (0.98 and 1.05 A). A mutant complex that changes the Asp to an Asn, which forms a normal hydrogen bond, has a similar free energy of binding to the wild type complex, suggesting that the contribution of the short hydrogen bond is not extraordinarily strong.

A low energy short hydrogen bond in very high resolution structures of protein receptor--phosphate complexes.,Wang Z, Luecke H, Yao N, Quiocho FA Nat Struct Biol. 1997 Jul;4(7):519-22. PMID:9228942^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Wang Z, Luecke H, Yao N, Quiocho FA. A low energy short hydrogen bond in very high resolution structures of protein receptor--phosphate complexes. Nat Struct Biol. 1997 Jul;4(7):519-22. PMID:9228942

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OCA

[1] Wang Z, Luecke H, Yao N, Quiocho FA. A low energy short hydrogen bond in very high resolution structures of protein receptor--phosphate complexes. Nat Struct Biol. 1997 Jul;4(7):519-22. PMID:9228942

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