3it3 Summary


Crystal Structure Francisella tularensis histidine acid phosphatase D261A mutant complexed with substrate 3'-AMP

The structure was published by Singh, H., Felts, R.L., Schuermann, J.P., Reilly, T.J., and Tanner, J.J., in 2009 in a paper entitled "Crystal Structures of the histidine acid phosphatase from Francisella tularensis provide insight into substrate recognition." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.5 Å and deposited in 2009.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of Acid phosphatase.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule most likely forms homodimers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Acid phosphatase Q2A612 (17-351) (Q2A612_FRATH)search Francisella tularensis subsp. holarctica LVSsearch 95% 342 98%
B Acid phosphatase Q2A612 (17-351) (Q2A612_FRATH)search Francisella tularensis subsp. holarctica LVSsearch 95% 342 98%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q2A612 (17 - 351) Acid phosphatase Francisella tularensis subsp. holarctica LVS

Chain Sequence family (Pfam)
A, B (Q2A612) PF00328: Histidine phosphatase superfamily (branch 2)search

Chain ID Molecular function (GO) Biological process (GO)
A, B (Q2A612) acid phosphatase activitysearch hydrolase activitysearch dephosphorylationsearch metabolic processsearch

Chain InterPro annotation
A, B Histidine phosphatase superfamily, clade-2search Histidine phosphatase superfamilysearch