Histidine ammonia-lyase (HAL) from Pseudomonas putida
The structure was published by Schwede, T.F., Retey, J., and Schulz, G.E., in 1999 in a paper entitled "Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.1 Å and deposited in 1999.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of Histidine ammonia-lyase. This molecule has the UniProt identifier P21310 (HUTH_PSEPU). The sample contained 507 residues which is 99% of the natural sequence. Out of 507 residues 507 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 homotetramers.
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: