1dw9 Summary

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STRUCTURE OF CYANASE REVEALS THAT A NOVEL DIMERIC AND DECAMERIC ARRANGEMENT OF SUBUNITS IS REQUIRED FOR FORMATION OF THE ENZYME ACTIVE SITE

The structure was published by Walsh, M.A., Otwinowski, Z., Perrakis, A., Anderson, P.M., and Joachimiak, A., in 2000 in a paper entitled "Structure of Cyanase Reveals that a Novel Dimeric and Decameric Arrangement of Subunits is Required for Formation of the Enzyme Active Site" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.65 Å and deposited in 1999.

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

This PDB entry contains multiple copies of the structure of CYANATE LYASE.

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 homodecamers.

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 CYANATE LYASE P00816 (1-156) (CYNS_ECOLI)search Escherichia coli K-12search 100% 156 100%
B CYANATE LYASE P00816 (1-156) (CYNS_ECOLI)search Escherichia coli K-12search 100% 156 100%
C CYANATE LYASE P00816 (1-156) (CYNS_ECOLI)search Escherichia coli K-12search 100% 156 100%
D CYANATE LYASE P00816 (1-156) (CYNS_ECOLI)search Escherichia coli K-12search 100% 156 100%
E CYANATE LYASE P00816 (1-156) (CYNS_ECOLI)search Escherichia coli K-12search 100% 156 100%
F CYANATE LYASE P00816 (1-156) (CYNS_ECOLI)search Escherichia coli K-12search 100% 156 100%
G CYANATE LYASE P00816 (1-156) (CYNS_ECOLI)search Escherichia coli K-12search 100% 156 100%
H CYANATE LYASE P00816 (1-156) (CYNS_ECOLI)search Escherichia coli K-12search 100% 156 100%
I CYANATE LYASE P00816 (1-156) (CYNS_ECOLI)search Escherichia coli K-12search 100% 156 100%
J CYANATE LYASE P00816 (1-156) (CYNS_ECOLI)search Escherichia coli K-12search 100% 156 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P00816 (1 - 156) CYANATE LYASE Escherichia coli

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B, C, D, E, F, G, H, I, J (P00816) Cyanase N-terminal domainsearch, Cyanase C-terminal domainsearch lambda repressor-like DNA-binding domainssearch, Cyanate Lyase; Chain: A, domain 2search PF02560: Cyanate lyase C-terminal domainsearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A, B, C, D, E, F, G, H, I, J (P00816) cyanate hydratase activitysearch DNA bindingsearch lyase activitysearch cyanate metabolic processsearch cyanate catabolic processsearch cytoplasmsearch

Chain InterPro annotation
A, B, C, D, E, F, G, H, I, J Cyanate lyase, C-terminalsearch Cyanate hydratasesearch Lambda repressor-like, DNA-binding domainsearch