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Structure of PDB 5o5c Chain C

Receptor sequence >5o5cC (length=462) Species: 665029 (Erwinia amylovora CFBP1430) [Search protein sequence] PHDFIFNDHQLSAWARQTEQVLALMTETVKGVEKPFSGILPHELAREFSG VDLDQGSNEAALEELKKLYLRDAVWFHHPKYVAHLNCPVVLPSLLAEQIM AAVNSSVDTWDQSAGGTLIEQKVIDWTLSRIGLPAGADGIFTSGGTQSNL MAMLLARDSWCAAHHPGHLIKHRGLPHDAAKWRVFTSKLSHFSIQKSMAI LGLGYDAVIPVDYDERYRMDVDCLKQEVQRCLQQGLIPVAVVATSGTTDF GSIDPLGAISELCKHHGMWMHVDAAYGCGLLVSESHRPRLAGIEKADSVT VDYHKSFFQTVSCGAFFVRDKHHLSHVTGTPNLVNKSIQTTRRFDALKMW LTLRVSGPMALGNAFDDILALTQIAHQLLNAHPAIEVLHVPELTTQIFRY VPALTDEINTNIRKAVFRSGNAVIAGTKVNGRQYLKFTLLNPNTTAADIE DVIALIVHYGRE

3D structure PDB 5o5c A complete structural characterization of the desferrioxamine E biosynthetic pathway from the fire blight pathogen Erwinia amylovora. Chain C 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 C G167 G168 T169 H214 T271 D296 A298 D325 H327 K328 G144 G145 T146 H191 T248 D273 A275 D302 H304 K305

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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