Structure of PDB 1g1l Chain B Binding Site BS02

Receptor Information
>1g1l Chain B (length=293) Species: 287 (Pseudomonas aeruginosa) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MKRKGIILAGGSGTRLHPATLAISKQLLPVYDKPMIYYPLSTLMLAGIRE
ILIISTPQDTPRFQQLLGDGSNWGLDLQYAVQPSPDGLAQAFLIGESFIG
NDLSALVLGDNLYYGHDFHELLGSASQRQTGASVFAYHVLDPERYGVVEF
DQGGKAISLEEKPLEPKSNYAVTGLYFYDQQVVDIARDLKPSPRGELEIT
DVNRAYLERGQLSVEIMGRGYAWLDTGTHDSLLEAGQFIATLENRQGLKV
ACPEEIAYRQKWIDAAQLEKLAAPLAKNGYGQYLKRLLTETVY
Ligand information
Ligand IDDAU
InChIInChI=1S/C16H26N2O16P2/c1-6-3-18(16(25)17-14(6)24)10-2-7(20)9(31-10)5-30-35(26,27)34-36(28,29)33-15-13(23)12(22)11(21)8(4-19)32-15/h3,7-13,15,19-23H,2,4-5H2,1H3,(H,26,27)(H,28,29)(H,17,24,25)/t7-,8+,9+,10+,11+,12-,13+,15+/m0/s1
InChIKeyYSYKRGRSMLTJNL-URARBOGNSA-N
SMILES
SoftwareSMILES
CACTVS 3.370CC1=CN([CH]2C[CH](O)[CH](CO[P](O)(=O)O[P](O)(=O)O[CH]3O[CH](CO)[CH](O)[CH](O)[CH]3O)O2)C(=O)NC1=O
OpenEye OEToolkits 1.7.6CC1=CN(C(=O)NC1=O)C2CC(C(O2)COP(=O)(O)OP(=O)(O)OC3C(C(C(C(O3)CO)O)O)O)O
CACTVS 3.370CC1=CN([C@H]2C[C@H](O)[C@@H](CO[P](O)(=O)O[P](O)(=O)O[C@H]3O[C@H](CO)[C@@H](O)[C@H](O)[C@H]3O)O2)C(=O)NC1=O
OpenEye OEToolkits 1.7.6CC1=CN(C(=O)NC1=O)[C@H]2C[C@@H]([C@H](O2)CO[P@](=O)(O)O[P@](=O)(O)O[C@@H]3[C@@H]([C@H]([C@@H]([C@H](O3)CO)O)O)O)O
ACDLabs 12.01O=C1C(=CN(C(=O)N1)C2OC(C(O)C2)COP(=O)(OP(=O)(OC3OC(C(O)C(O)C3O)CO)O)O)C
FormulaC16 H26 N2 O16 P2
Name2'DEOXY-THYMIDINE-5'-DIPHOSPHO-ALPHA-D-GLUCOSE
ChEMBLCHEMBL412989
DrugBankDB03751
ZINC
PDB chain1g1l Chain B Residue 3503 [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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PDB1g1l The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate thymidylyltransferase (RmlA).
Resolution1.77 Å
Binding residue
(original residue number in PDB)		Y114 G115 H116 D117 F118 H119 E120 V250 E255 I256 R259 Y293
Binding residue
(residue number reindexed from 1)		Y114 G115 H116 D117 F118 H119 E120 V250 E255 I256 R259 Y293
Annotation score4
Enzymatic activity
Enzyme Commision number 2.7.7.24: glucose-1-phosphate thymidylyltransferase.
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0008879 glucose-1-phosphate thymidylyltransferase activity
GO:0016779 nucleotidyltransferase activity
GO:0046872 metal ion binding
Biological Process
GO:0009058 biosynthetic process
GO:0009244 lipopolysaccharide core region biosynthetic process
GO:0019305 dTDP-rhamnose biosynthetic process
GO:0045226 extracellular polysaccharide biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1g1l, PDBe:1g1l, PDBj:1g1l
PDBsum1g1l
PubMed11118200
UniProtQ9HU22

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