Structure of PDB 1ket Chain A

Receptor sequence

>1ketA (length=346) Species: 1307 (Streptococcus suis)

QFKNIIVTGGAGFIGSNFVHYVYNNHPDVHVTVLDKLTYAGNKANLEAIL
GDRVELVVGDIADAELVDKLAAKADAIVHYAAESHNDNSLNDPSPFIHTN
FIGTYTLLEAARKYDIRFHHVSTDEVYGDLPLREDLPGHGEGPGEKFTAE
TNYNPSSPYSSTKAASDLIVKAWVRSFGVKATISNCSNNYGPYQHIEKFI
PRQITNILAGIKPKLYGEGKNVRDWIHTNDHSTGVWAILTKGRMGETYLI
GADGEKNNKEVLELILEKMGQPKDAYDHVTDRAGHDLRYAIDASKLRDEL
GWTPQFTDFSEGLEETIQWYTDNQDWWKAEKEAVEANYAKTQEVIK

3D structure

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

Enzymatic activity

• Catalytic site (original residue number in PDB): T125 D126 E127 Y161 K165
• Catalytic site (residue number reindexed from 1): T123 D124 E125 Y159 K163
• 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	A	E127 N190 F201 R204 Q205 K216 Y218 R225 N260 R284 H287	E125 N188 F199 R202 Q203 K214 Y216 R223 N258 R282 H285
BS02	NAD	A	G14 F15 I16 D37 K38 L39 T40 A42 G43 D62 I63 Y82 A84 S86 T101 S124 T125 Y161 K165	G12 F13 I14 D35 K36 L37 T38 A40 G41 D60 I61 Y80 A82 S84 T99 S122 T123 Y159 K163

Gene Ontology

Molecular Function

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

Biological Process

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

External links

• PDB: RCSB:1ket, PDBe:1ket, PDBj:1ket
• PDBsum: 1ket
• PubMed: 11796113
• UniProt: P95780|RMLB_STRMU dTDP-glucose 4,6-dehydratase (Gene Name=rmlB)