1im5 Summary


Crystal Structure of Pyrazinamidase of Pyrococcus horikoshii in Complex with Zinc

The structure was published by Du, X., Wang, W., Kim, R., Yakota, H., Nguyen, H., and Kim, S.H., in 2001 in a paper entitled "Crystal structure and mechanism of catalysis of a pyrazinamidase from Pyrococcus horikoshii." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.65 Å and deposited in 2001.

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

The PDB entry contains the structure of 180aa long hypothetical Pyrazinamidase/Nicotinamidase. This molecule has the UniProt identifier O58727 (O58727_PYRHO)search. The sample contained 180 residues which is 100% of the natural sequence. Out of 180 residues 179 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 is most likely monomeric.

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 180aa long hypothetical Pyrazinamidase/Nicotinamidase O58727 (1-180) (O58727_PYRHO)search Pyrococcus horikoshii OT3search 100% 180 99%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
O58727 (1 - 180) 180aa long hypothetical Pyrazinamidase/Nicotinamidase Pyrococcus horikoshii

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (O58727) Isochorismatase-like hydrolasessearch Rossmann foldsearch PF00857: Isochorismatase familysearch

Chain ID Molecular function (GO) Biological process (GO)
A (O58727) catalytic activitysearch metal ion bindingsearch metabolic processsearch

Chain InterPro annotation
A Isochorismatase-likesearch