4Z5S

Crystal structure of apo-form of aldehyde deformylating oxygenase from Synechocystis sp.PCC 6803

Summary for 4Z5S

Entry DOI	10.2210/pdb4z5s/pdb
Descriptor	Aldehyde decarbonylase (2 entities in total)
Functional Keywords	oxygenase, lyase
Biological source	Synechocystis sp. (strain PCC 6803 / Kazusa)
Total number of polymer chains	1
Total formula weight	26202.65
Authors	Jia, C.,Li, M.,Chang, W. (deposition date: 2015-04-03, release date: 2016-04-06, Last modification date: 2023-11-08)
Primary citation	Wang, Q.,Bao, L.,Jia, C.,Li, M.,Li, J.J.,Lu, X. Identification of residues important for the activity of aldehyde-deformylating oxygenase through investigation into the structure-activity relationship BMC Biotechnol., 17:31-31, 2017 Cited by PubMed Abstract: Aldehyde-deformylating oxygenase (ADO) is a key enzyme involved in the biosynthetic pathway of fatty alk(a/e)nes in cyanobacteria. However, cADO (cyanobacterial ADO) showed extreme low activity with the k value below 1 min, which would limit its application in biofuel production. To identify the activity related key residues of cADO is urgently required. PubMed: 28302170 DOI: 10.1186/s12896-017-0351-8 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.582 Å)

Structure validation