Structure of PDB 1kew Chain B

Receptor sequence

>1kewB (length=361) Species: 90371 (Salmonella enterica subsp. enterica serovar Typhimurium)

MKILITGGAGFIGSAVVRHIIKNTQDTVVNIDKLTYAGNLESLSDISESN
RYNFEHADICDSAEITRIFEQYQPDAVMHLAAESHVDRSITGPAAFIETN
IVGTYALLEVARKYWSALGEDKKNNFRFHHISTDEVYGDLPHPDEVENSV
TLPLFTETTAYAPSSPYSASKASSDHLVRAWRRTYGLPTIVTNCSNNYGP
YHFPEKLIPLVILNALEGKPLPIYGKGDQIRDWLYVEDHARALHMVVTEG
KAGETYNIGGHNEKKNLDVVFTICDLLDEIVPKATSYREQITYVADRPGH
DRRYAIDAGKISRELGWKPLETFESGIRKTVEWYLANTQWVNNVKSGAYQ
SWIEQNYEGRQ

3D structure

• PDB: 1kew Toward a structural understanding of the dehydratase mechanism.
• Chain: B
• Resolution: 1.8 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): T133 D134 E135 L152 L154 F155 T158 Y167 K171
• Catalytic site (residue number reindexed from 1): T133 D134 E135 L152 L154 F155 T158 Y167 K171
• Enzyme Commision number: 4.2.1.46: dTDP-glucose 4,6-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	TYD	B	E135 N196 K206 L207 P222 Y224 R231 N266 R297 H300 Y357	E135 N196 K206 L207 P222 Y224 R231 N266 R297 H300 Y357
BS02	NAD	B	G10 F11 I12 D32 K33 L34 T35 A37 G38 D58 I59 L80 A81 A82 S84 T99 I131 S132 T133 Y167 K171 C194 N196	G10 F11 I12 D32 K33 L34 T35 A37 G38 D58 I59 L80 A81 A82 S84 T99 I131 S132 T133 Y167 K171 C194 N196

Gene Ontology

Molecular Function

• GO:0008460 dTDP-glucose 4,6-dehydratase activity
• GO:0016829 lyase activity
• GO:0070404 NADH binding

Biological Process

• GO:0009103 lipopolysaccharide biosynthetic process
• GO:0009225 nucleotide-sugar metabolic process
• GO:0009243 O antigen biosynthetic process
• GO:0019305 dTDP-rhamnose biosynthetic process
• GO:0045226 extracellular polysaccharide biosynthetic process

External links

• PDB: RCSB:1kew, PDBe:1kew, PDBj:1kew
• PDBsum: 1kew
• PubMed: 11796113
• UniProt: P26391|RMLB_SALTY dTDP-glucose 4,6-dehydratase (Gene Name=rfbB)