Structure of PDB 1wvg Chain B

Receptor sequence
>1wvgB (length=350) Species: 220341 (Salmonella enterica subsp. enterica serovar Typhi str. CT18) [Search protein sequence]
SIDKNFWQGKRVFVTGHTGFKGSWLSLWLTEMGAIVKGYALDAPTVPSLF
EIVRLNDLMESHIGDIRDFEKLRSSIAEFKPEIVFHMAAQPLVRLSYEQP
IKTYSTNVMGTVHLLETVKQVGNIKAVVNITSDKCYDNREWVWGYRENEP
MGGYDPYSNSKGCAELVASAFRNSFFNPANQHGVGLASVRAGNVIGGGDW
AKDRLIPDILRSFENNQQVIIRNPYSIRPWQHVLEPLSGYIVVAQRLYTE
GAKFSEGWNFGPRDEDAKTVEFIVDKMVTLWGDASWLLDGENHPHHYLKL
DCSKANMQLGWHPRWGLTETLSRIVKWHKAWIRGEDMLICSKREISDYMS
3D structure
PDB1wvg Structure of CDP-D-glucose 4,6-dehydratase from Salmonella typhi complexed with CDP-D-xylose.
ChainB
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) T1133 S1134 D1135 K1136 Y1159 K1163
Catalytic site (residue number reindexed from 1) T131 S132 D133 K134 Y157 K161
Enzyme Commision number 4.2.1.45: CDP-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 APR B G1018 T1020 G1021 F1022 K1023 A1042 L1043 P1046 D1067 I1068 M1089 A1090 A1091 P1093 I1132 Y1159 K1163 G16 T18 G19 F20 K21 A40 L41 P44 D65 I66 M87 A88 A89 P91 I130 Y157 K161
Gene Ontology
Molecular Function
GO:0016829 lyase activity
GO:0047733 CDP-glucose 4,6-dehydratase activity
Biological Process
GO:0009103 lipopolysaccharide biosynthetic process
GO:0009243 O antigen biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1wvg, PDBe:1wvg, PDBj:1wvg
PDBsum1wvg
PubMed15805590
UniProtP26397|RFBG_SALTY CDP-glucose 4,6-dehydratase (Gene Name=rfbG)

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