4bvt Summary

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PDB entry 4bvt (supersedes 3zgu)

Cyanuric acid hydrolase: evolutionary innovation by structural concatenation.

The structure was published by Peat, T.S., Balotra, S., Wilding, M., et al., Cowieson, N., Newman, J., and Scott, C., in 2013 in a paper entitled "Cyanuric Acid Hydrolase: Evolutionary Innovation by Structural Concatenation." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 3.1 Å and deposited in 2013.

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

This PDB entry contains multiple copies of the structure of CYANURIC ACID AMIDOHYDROLASE.

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 CYANURIC ACID AMIDOHYDROLASE P58329 (1-363) (ATZD_PSESD)search Pseudomonas sp. ADPsearch 100% 383 95%
B CYANURIC ACID AMIDOHYDROLASE P58329 (1-363) (ATZD_PSESD)search Pseudomonas sp. ADPsearch 100% 383 95%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P58329 (1 - 363) CYANURIC ACID AMIDOHYDROLASE Pseudomonas sp. ADP

Chain Sequence family (Pfam)
A, B (P58329) PF09663: Amidohydrolase ring-opening protein (Amido_AtzD_TrzD)search

Chain ID Biological process (GO) Molecular function (GO)
A, B (P58329) atrazine catabolic processsearch hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidessearch cyanuric acid amidohydrolase activitysearch hydrolase activitysearch

Chain InterPro annotation
A, B Cyanuric acid hydrolase/Barbiturasesearch