Structure of PDB 5o5c Chain B

Receptor sequence
>5o5cB (length=468) Species: 665029 (Erwinia amylovora CFBP1430) [Search protein sequence]
PHDFIFNDHQLSAWARQTEQVLALMTETVKGVEKPFSGILPHELAREFSG
VDLDQGSNEAALEELKKLYLRDAVWFHHPKYVAHLNCPVVLPSLLAEQIM
AAVNSSVDTWDQSAGGTLIEQKVIDWTLSRIGLPAGADGIFTSGGTQSNL
MAMLLARDSWCAAHHPGHLIKHRGLPHDAAKWRVFTSKLSHFSIQKSMAI
LGLGYDAVIPVDYDERYRMDVDCLKQEVQRCLQQGLIPVAVVATSGTTDF
GSIDPLGAISELCKHHGMWMHVDAAYGCGLLVSESHRPRLAGIEKADSVT
VDYHKSFFQTVSCGAFFVRDKHHLSHVTGTPNLVNKSIQTTRRFDALKMW
LTLRVSGPMALGNAFDDILALTQIAHQLLNAHPAIEVLHVPELTTQIFRY
VPDALTDEINTNIRKAVFRSGNAVIAGTKVNGRQYLKFTLLNPNTTAADI
EDVIALIVHYGREQVRGP
3D structure
PDB5o5c A complete structural characterization of the desferrioxamine E biosynthetic pathway from the fire blight pathogen Erwinia amylovora.
ChainB
Resolution2.1 Å
3D
structure
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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 B T377 T378 T340 T341
BS02 PLP B G168 T169 H214 T271 D296 A298 D325 H327 K328 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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5o5c, PDBe:5o5c, PDBj:5o5c
PDBsum5o5c
PubMed29428557
UniProtD4I245

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