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Structure of PDB 5o5c Chain E

Receptor sequence >5o5cE (length=457) Species: 665029 (Erwinia amylovora CFBP1430) [Search protein sequence] HDFIFNDHQLSAWARQTEQVLALMTETVKGVEKPFSGILPHELAREFSGV DLDQGSNEAALEELKKLYLRDAVWFHHPKYVAHLNCPVVLPSLLAEQIMA AVNSSVDTWDQSAGGTLIEQKVIDWTLSRIGLPAGADGIFTSGGTQSNLM AMLLARDSWCAAHHPGHLIKHRGLPHDAAKWRVFTSKLSHFSIQKSMAIL GLGYDAVIPVDYDERYRMDVDCLKQEVQRCLQQGLIPVAVVATSGTTDFG SIDPLGAISELCKHHGMWMHVDAAYGCGLLVSESHRPRLAGIEKADSVTV DYHKSFFQTVSCGAFFVRDKHHLSHVTSIQTTRRFDALKMWLTLRVSGPM ALGNAFDDILALTQIAHQLLNAHPAIEVLHVPELTTQIFRYVPALTDEIN TNIRKAVFRSGNAVIAGTKVNGRQYLKFTLLNPNTTAADIEDVIALIVHY GREQVRG

3D structure PDB 5o5c A complete structural characterization of the desferrioxamine E biosynthetic pathway from the fire blight pathogen Erwinia amylovora. Chain E Resolution 2.1 Å 3D structure [Spin on] [Spin off] [Reset orientation] [High quality] [Low quality] [White background] [Black background] [Download] [Download structure with residue number starting from 1]

Enzymatic activity Enzyme Commision number 4.1.1.-

Interaction with ligand Site # Ligand Ligand chain Binding residues on receptor (original residue number in PDB) Binding residues on receptor (residue number reindexed from 1) Binding affinity BS01 PLP E G168 T169 H214 T271 D296 A298 D325 H327 K328 G144 T145 H190 T247 D272 A274 D301 H303 K304

Gene Ontology Molecular Function GO:0016829 lyase activity GO:0016830 carbon-carbon lyase activity GO:0016831 carboxy-lyase activity GO:0030170 pyridoxal phosphate binding

	Biological Process
GO:0019752	carboxylic acid metabolic process

	Cellular Component
GO:0005737	cytoplasm

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