Lactobacillus casei HprK/P Bound to Phosphate
The structure was published by Fieulaine, S., Morera, S., Poncet, S., et al., Janin, J., Deutscher, J., and Nessler, S., in 2001 in a paper entitled "X-ray structure of HPr kinase: a bacterial protein kinase with a P-loop nucleotide-binding domain." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.8 Å and deposited in 2001.
The experimental data on which the structure is based was not deposited.
The PDB entry contains the structure of HPRK PROTEIN. This molecule has the UniProt identifier Q9RE09 (HPRK_LACCA). The sample contained 205 residues which is < 90% of the natural sequence. Out of 205 residues 154 were observed and are deposited in the PDB.
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 homohexamers.
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):
This entry contains 1 unique UniProt protein: