1b8f Summary


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)search. 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):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Histidine ammonia-lyase P21310 (2-510) (HUTH_PSEPU)search Pseudomonas putidasearch 99% 507 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P21310 (2 - 510) Histidine ammonia-lyase Pseudomonas putida

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P21310) HAL/PAL-likesearch Fumarase/aspartase (N-terminal domain)search, Fumarase/aspartase (Central domain)search PF00221: Aromatic amino acid lyasesearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A (P21310) histidine ammonia-lyase activitysearch lyase activitysearch catalytic activitysearch ammonia-lyase activitysearch biosynthetic processsearch histidine metabolic processsearch histidine catabolic processsearch histidine catabolic process to glutamate and formatesearch histidine catabolic process to glutamate and formamidesearch cytoplasmsearch

Chain InterPro annotation
A Aromatic amino acid lyasesearch Histidine ammonia-lyasesearch L-Aspartase-likesearch Phenylalanine/histidine ammonia-lyases, active sitesearch Fumarase/histidase, N-terminalsearch