Structure of PDB 7kws Chain B Binding Site BS02

Receptor Information
>7kws Chain B (length=387) Species: 192222 (Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MKIVIVGIGYVGLANAILFSKNNENEVVLLDIDENKIQSINNHKSPIKDK
LIEKFFVQSKLHATSNIKEAYFNADFAVIATPTDYDENFFDTRSIENVLK
DIKNINSKINVIIKSTVPIGYTKTIKQKFNMSNIVFSPEFLREGSALYDS
LYPSRIIIGDKSVLGKTIGDLFLKNIEKKNVDIFYMDSDEAESVKLFSNT
YLAMRVGFFNEVDSYARKHNLNSADIIKGISADDRIGKYYNNPSFGYGGY
CLPKDTKQLLANFYNIPNSLIKAIVETNEIRKKFITQLILEKKPNILGIY
RLIMKQNSDNFRNSVIIDIIKYLQEYNSNIELIIYEPLVKEKKFLNIKVE
NDFNVFGAKVDLIIANRFDDKLKEIKDKVFSADVFYT
Ligand information
Ligand IDNAD
InChIInChI=1S/C21H27N7O14P2/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(32)14(30)11(41-21)6-39-44(36,37)42-43(34,35)38-5-10-13(29)15(31)20(40-10)27-3-1-2-9(4-27)18(23)33/h1-4,7-8,10-11,13-16,20-21,29-32H,5-6H2,(H5-,22,23,24,25,33,34,35,36,37)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1
InChIKeyBAWFJGJZGIEFAR-NNYOXOHSSA-N
SMILES
SoftwareSMILES
CACTVS 3.341NC(=O)c1ccc[n+](c1)[C@@H]2O[C@H](CO[P]([O-])(=O)O[P@](O)(=O)OC[C@H]3O[C@H]([C@H](O)[C@@H]3O)n4cnc5c(N)ncnc45)[C@@H](O)[C@H]2O
OpenEye OEToolkits 1.5.0c1cc(c[n+](c1)C2C(C(C(O2)COP(=O)([O-])OP(=O)(O)OCC3C(C(C(O3)n4cnc5c4ncnc5N)O)O)O)O)C(=O)N
CACTVS 3.341NC(=O)c1ccc[n+](c1)[CH]2O[CH](CO[P]([O-])(=O)O[P](O)(=O)OC[CH]3O[CH]([CH](O)[CH]3O)n4cnc5c(N)ncnc45)[CH](O)[CH]2O
OpenEye OEToolkits 1.5.0c1cc(c[n+](c1)[C@H]2[C@@H]([C@@H]([C@H](O2)CO[P@@](=O)([O-])O[P@@](=O)(O)OC[C@@H]3[C@H]([C@H]([C@@H](O3)n4cnc5c4ncnc5N)O)O)O)O)C(=O)N
FormulaC21 H27 N7 O14 P2
NameNICOTINAMIDE-ADENINE-DINUCLEOTIDE
ChEMBLCHEMBL1234613
DrugBankDB14128
ZINC
PDB chain7kws Chain B Residue 402 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB7kws Functional and Structural Characterization of the UDP-Glucose Dehydrogenase Involved in Capsular Polysaccharide Biosynthesis from Campylobacter jejuni .
Resolution2.09 Å
Binding residue
(original residue number in PDB)		G7 G9 Y10 V11 D31 I32 T83 P84 T85 T120 E143 E147 Y254 C255 R316
Binding residue
(residue number reindexed from 1)		G7 G9 Y10 V11 D31 I32 T81 P82 T83 T116 E139 E143 Y250 C251 R312
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) T120 E147 K199 N203 C255 D259
Catalytic site (residue number reindexed from 1) T116 E143 K195 N199 C251 D255
Enzyme Commision number 1.1.1.22: UDP-glucose 6-dehydrogenase.
Gene Ontology
Molecular Function
GO:0003979 UDP-glucose 6-dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
GO:0051287 NAD binding
Biological Process
GO:0000271 polysaccharide biosynthetic process
GO:0006065 UDP-glucuronate biosynthetic process
GO:0045227 capsule polysaccharide biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:7kws, PDBe:7kws, PDBj:7kws
PDBsum7kws
PubMed33621065
UniProtQ0P8H3|UDG_CAMJE UDP-glucose 6-dehydrogenase (Gene Name=kfiD)

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