Structure of PDB 3ekg Chain B

Receptor sequence
>3ekgB (length=395) Species: 322710 (Azotobacter vinelandii DJ) [Search protein sequence]
SLSIPTIKQVRAFVLRGGGADYHDQGDGHWIDDHISTPMGKYPEYRQSRR
SFGINVLGTLVVEIEASDGNVGFAVTTGGEPAAYIVEKHLARFLEGARVT
DIERIWDQMYNSTLYYGRKGLVINTISGVDLALWDLLGKVRREPVHQLLG
GAVRDELQFYATGARPDLAQKMGFIGGKMPLHHGPSEGEEGLKKNLEELA
TMRERVGPDFWLMFDCWMSLDLNYATRLARGAREYGLKWIEEALPPDDYW
GYAELRRNAPTGMMVTTGEHEATRWGFRMLLEMGCCDIIQPDVGWCGGVT
ELLKISALADAHNALVVPHGSSVYSYHFVATRQNSPFAEFLMMAPKADQV
VPMFHPQLLGEPVPENGRMRLSRLDQPGFGVTLNPECQLHRPYTH
3D structure
PDB3ekg CRYSTAL STRUCTURE OF L-RHAMNONATE DEHYDRATASE FROM AZOTOBACTER VINELANDII complexed with Mg and L-TARTRATE
ChainB
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K179 P181 G185 S187 E191 D216 W218 E242 T267 G269 E270 Q291 D293 H320 E340 D349
Catalytic site (residue number reindexed from 1) K178 P180 G184 S186 E190 D215 W217 E241 T266 G268 E269 Q290 D292 H319 E339 D348
Enzyme Commision number 4.2.1.90: L-rhamnonate dehydratase.
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 MG B D216 E242 E270 D215 E241 E269
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0016829 lyase activity
GO:0016836 hydro-lyase activity
GO:0046872 metal ion binding
GO:0050032 L-rhamnonate dehydratase activity
Biological Process
GO:0009063 amino acid catabolic process
GO:0016052 carbohydrate catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3ekg, PDBe:3ekg, PDBj:3ekg
PDBsum3ekg
PubMed
UniProtC1DMY1

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