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Receptor Information

>1g3l Chain A (length=292) Species: 287 (Pseudomonas aeruginosa) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

KRKGIILAGGSGTRLHPATLAISKQLLPVYDKPMIYYPLSTLMLAGIREI
LIISTPQDTPRFQQLLGDGSNWGLDLQYAVQPSPDGLAQAFLIGESFIGN
DLSALVLGDNLYYGHDFHELLGSASQRQTGASVFAYHVLDPERYGVVEFD
QGGKAISLEEKPLEPKSNYAVTGLYFYDQQVVDIARDLKPSPRGELEITD
VNRAYLERGQLSVEIMGRGYAWLDTGTHDSLLEAGQFIATLENRQGLKVA
CPEEIAYRQKWIDAAQLEKLAAPLAKNGYGQYLKRLLTETVY

Ligand ID

TRH

InChI

InChI=1S/C16H26N2O15P2/c1-6-4-18(16(24)17-14(6)23)10-3-8(19)9(31-10)5-29-34(25,26)33-35(27,28)32-15-13(22)12(21)11(20)7(2)30-15/h4,7-13,15,19-22H,3,5H2,1-2H3,(H,25,26)(H,27,28)(H,17,23,24)/t7-,8-,9+,10+,11-,12+,13+,15+/m0/s1

InChIKey

ZOSQFDVXNQFKBY-CGAXJHMRSA-N

SMILES

Software	SMILES
OpenEye OEToolkits 1.5.0	CC1C(C(C(C(O1)OP(=O)(O)OP(=O)(O)OCC2C(CC(O2)N3C=C(C(=O)NC3=O)C)O)O)O)O
CACTVS 3.341	C[CH]1O[CH](O[P](O)(=O)O[P](O)(=O)OC[CH]2O[CH](C[CH]2O)N3C=C(C)C(=O)NC3=O)[CH](O)[CH](O)[CH]1O
CACTVS 3.341	C[C@@H]1O[C@H](O[P@@](O)(=O)O[P@](O)(=O)OC[C@H]2O[C@H](C[C@@H]2O)N3C=C(C)C(=O)NC3=O)[C@H](O)[C@H](O)[C@H]1O
ACDLabs 10.04	O=P(OC1OC(C(O)C(O)C1O)C)(O)OP(=O)(O)OCC3OC(N2C=C(C(=O)NC2=O)C)CC3O
OpenEye OEToolkits 1.5.0	C[C@H]1[C@@H]([C@H]([C@H]([C@H](O1)O[P@](=O)(O)O[P@@](=O)(O)OC[C@@H]2[C@H](C[C@@H](O2)N3C=C(C(=O)NC3=O)C)O)O)O)O

Formula

C16 H26 N2 O15 P2

Name

2'-DEOXY-THYMIDINE-BETA-L-RHAMNOSE

PDB chain

1g3l Chain C Residue 505 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	1g3l The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate thymidylyltransferase (RmlA).
Resolution	2.7 Å
Binding residue (original residue number in PDB)	G218 R219 G220
Binding residue (residue number reindexed from 1)	G217 R218 G219
Annotation score	3

Enzyme Commision number

2.7.7.24: glucose-1-phosphate thymidylyltransferase.

	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

PDB	RCSB:1g3l, PDBe:1g3l, PDBj:1g3l
PDBsum	1g3l
PubMed	11118200
UniProt	Q9HU22

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Structure of PDB 1g3l Chain A Binding Site BS03