Structure of PDB 1kep Chain A

Receptor sequence
>1kepA (length=346) Species: 1307 (Streptococcus suis) [Search protein sequence]
QFKNIIVTGGAGFIGSNFVHYVYNNHPDVHVTVLDKLTYAGNKANLEAIL
GDRVELVVGDIADAELVDKLAAKADAIVHYAAESHNDNSLNDPSPFIHTN
FIGTYTLLEAARKYDIRFHHVSTDEVYGDLPLREDLPGHGEGPGEKFTAE
TNYNPSSPYSSTKAASDLIVKAWVRSFGVKATISNCSNNYGPYQHIEKFI
PRQITNILAGIKPKLYGEGKNVRDWIHTNDHSTGVWAILTKGRMGETYLI
GADGEKNNKEVLELILEKMGQPKDAYDHVTDRAGHDLRYAIDASKLRDEL
GWTPQFTDFSEGLEETIQWYTDNQDWWKAEKEAVEANYAKTQEVIK
3D structure
PDB1kep Toward a structural understanding of the dehydratase mechanism.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 NAD A G14 F15 I16 D37 K38 L39 T40 G43 D62 I63 Y82 A83 A84 S86 T101 S124 Y161 K165 N191 G12 F13 I14 D35 K36 L37 T38 G41 D60 I61 Y80 A81 A82 S84 T99 S122 Y159 K163 N189
BS02 TDX A S86 T125 E127 Y161 N190 K200 R225 R284 S84 T123 E125 Y159 N188 K198 R223 R282
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0008460 dTDP-glucose 4,6-dehydratase activity
GO:0016829 lyase activity
Biological Process
GO:0009225 nucleotide-sugar metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1kep, PDBe:1kep, PDBj:1kep
PDBsum1kep
PubMed11796113
UniProtQ8GIP9

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