1IXI

PHOSPHATE-BINDING PROTEIN MUTANT WITH ASP 56 REPLACED BY ASN COMPLEX WITH MONOBASIC PHOSPHATE ION

Summary for 1IXI

• Entry DOI: 10.2210/pdb1ixi/pdb
• Descriptor: PHOSPHATE-BINDING PROTEIN, DIHYDROGENPHOSPHATE ION (3 entities in total)
• Functional Keywords: phosphate transport, binding proteins, phosphate-binding, mutant
• Biological source: Escherichia coli
• Cellular location: Periplasm: P06128
• Total number of polymer chains: 1
• Total formula weight: 34553.60

Authors

Wang, Z.,Quiocho, F.A. (deposition date: 1996-10-17, release date: 1997-10-22, Last modification date: 2024-04-03)

Primary citation

Wang, Z.,Luecke, H.,Yao, N.,Quiocho, F.A.
A low energy short hydrogen bond in very high resolution structures of protein receptor--phosphate complexes.
Nat.Struct.Biol., 4:519-522, 1997

PubMed Abstract: 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.

PubMed: 9228942
DOI: 10.1038/nsb0797-519

Experimental method

X-RAY DIFFRACTION (1.89 Å)