Structure of PDB 1mbb Chain A Binding Site BS01

Receptor Information
>1mbb Chain A (length=340) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
HSLKPWNTFGIDHNAQHIVCAEDEQQLLNAWQYATAEGQPVLILGEGSNV
LFLEDYRGTVIINRIKGIEIHDEPDAWYLHVGAGENWHRLVKYTLQEGMP
GLENLALIPGCVGSSPIQNIGAYGVELQRVCAYVDSVELATGKQVRLTAK
ECRFGYRDSIFKHEYQDRFAIVAVGLRLPKEWQPVLTYGDLTRLDPTTVT
PQQVFNAVCHMRTTKLPDPKVNGNAGSFFKNPVVSAETAKALLSQFPTAP
NYPQADGSVKLAAGWLIDQCQLKGMQIGGAAVHRQQALVLINEDNAKSED
VVQLAHHVRQKVGEKFNVWLEPEVRFIGASGEVSAVETIS
Ligand information
Ligand IDEEB
InChIInChI=1S/C21H33N3O19P2/c1-3-9(19(31)32)39-17-13(22-8(2)26)20(41-10(6-25)15(17)29)42-45(36,37)43-44(34,35)38-7-11-14(28)16(30)18(40-11)24-5-4-12(27)23-21(24)33/h4-5,9-11,13-18,20,25,28-30H,3,6-7H2,1-2H3,(H,22,26)(H,31,32)(H,34,35)(H,36,37)(H,23,27,33)/t9-,10-,11-,13-,14-,15-,16-,17-,18-,20-/m1/s1
InChIKeyDFCARJAECCPPGB-LHYXAPFASA-N
SMILES
SoftwareSMILES
CACTVS 3.341CC[C@@H](O[C@H]1[C@H](O)[C@@H](CO)O[C@H](O[P@](O)(=O)O[P@@](O)(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)N3C=CC(=O)NC3=O)[C@@H]1NC(C)=O)C(O)=O
ACDLabs 10.04O=P(OC1OC(C(O)C(OC(C(=O)O)CC)C1NC(=O)C)CO)(O)OP(=O)(O)OCC3OC(N2C=CC(=O)NC2=O)C(O)C3O
OpenEye OEToolkits 1.5.0CCC(C(=O)O)O[C@@H]1[C@H]([C@H](O[C@@H]([C@H]1O)CO)O[P@@](=O)(O)O[P@](=O)(O)OC[C@@H]2[C@H]([C@H]([C@@H](O2)N3C=CC(=O)NC3=O)O)O)NC(=O)C
CACTVS 3.341CC[CH](O[CH]1[CH](O)[CH](CO)O[CH](O[P](O)(=O)O[P](O)(=O)OC[CH]2O[CH]([CH](O)[CH]2O)N3C=CC(=O)NC3=O)[CH]1NC(C)=O)C(O)=O
OpenEye OEToolkits 1.5.0CCC(C(=O)O)OC1C(C(OC(C1O)CO)OP(=O)(O)OP(=O)(O)OCC2C(C(C(O2)N3C=CC(=O)NC3=O)O)O)NC(=O)C
FormulaC21 H33 N3 O19 P2
NameURIDINE-DIPHOSPHATE-3(N-ACETYLGLUCOSAMINYL)BUTYRIC ACID
ChEMBL
DrugBank
ZINCZINC000038377582
PDB chain1mbb Chain A Residue 402 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1mbb (E)-enolbutyryl-UDP-N-acetylglucosamine as a mechanistic probe of UDP-N-acetylenolpyruvylglucosamine reductase (MurB).
Resolution2.3 Å
Binding residue
(original residue number in PDB)		A124 Y158 R159 Y190 G228 S229 P252 Y254 A264 G266 W267 D270 Q288 A289 E325
Binding residue
(residue number reindexed from 1)		A122 Y156 R157 Y188 G226 S227 P250 Y252 A262 G264 W265 D268 Q286 A287 E323
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) R159 S229 E325
Catalytic site (residue number reindexed from 1) R157 S227 E323
Enzyme Commision number 1.3.1.98: UDP-N-acetylmuramate dehydrogenase.
Gene Ontology
Molecular Function
GO:0008762 UDP-N-acetylmuramate dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0050660 flavin adenine dinucleotide binding
GO:0071949 FAD binding
Biological Process
GO:0008360 regulation of cell shape
GO:0009252 peptidoglycan biosynthetic process
GO:0051301 cell division
GO:0071555 cell wall organization
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1mbb, PDBe:1mbb, PDBj:1mbb
PDBsum1mbb
PubMed8634262
UniProtP08373|MURB_ECOLI UDP-N-acetylenolpyruvoylglucosamine reductase (Gene Name=murB)

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