Structure of PDB 1jut Chain B Binding Site BS03

Receptor Information
>1jut Chain B (length=264) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MKQYLELMQKVLDEGTQKNDRTGTGTLSIFGHQMRFNLQDGFPLVTTKRC
HLRSIIHELLWFLQGDTNIAYLHENNVTIWDEWADENGDLGPVYGKQWRA
WPTPDGRHIDQITTVLNQLKNDPDSRRIIVSAWNVGELDKMALAPCHAFF
QFYVADGKLSCQLYQRSCDVFLGLPFNIASYALLVHMMAQQCDLEVGDFV
WTGGDTHLYSNHMDQTHLQLSREPRPLPKLIIKRKPESIFDYRFEDFEIE
GYDPHPGIKAPVAI
Ligand information
Ligand IDLYD
InChIInChI=1S/C20H23N5O4/c1-10(2)15(19(28)29)23-17(26)12-6-3-11(4-7-12)5-8-13-9-22-16-14(13)18(27)25-20(21)24-16/h3-4,6-7,9-10,15H,5,8H2,1-2H3,(H,23,26)(H,28,29)(H4,21,22,24,25,27)/t15-/m0/s1
InChIKeyMYENGRJSPURSQB-HNNXBMFYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=C(O)C(NC(=O)c1ccc(cc1)CCc2cnc3N=C(NC(=O)c23)N)C(C)C
OpenEye OEToolkits 1.5.0CC(C)C(C(=O)O)NC(=O)c1ccc(cc1)CCc2c[nH]c3c2C(=O)NC(=N3)N
CACTVS 3.341CC(C)[C@H](NC(=O)c1ccc(CCc2c[nH]c3N=C(N)NC(=O)c23)cc1)C(O)=O
OpenEye OEToolkits 1.5.0CC(C)[C@@H](C(=O)O)NC(=O)c1ccc(cc1)CCc2c[nH]c3c2C(=O)NC(=N3)N
CACTVS 3.341CC(C)[CH](NC(=O)c1ccc(CCc2c[nH]c3N=C(N)NC(=O)c23)cc1)C(O)=O
FormulaC20 H23 N5 O4
Name2-{4-[2-(2-AMINO-4-OXO-4,7-DIHYDRO-3H-PYRROLO[2,3-D]PYRIMIDIN-5-YL)-ETHYL]-BENZOYLAMINO}-3-METHYL-BUTYRIC ACID;
LY338529
ChEMBL
DrugBankDB08131
ZINCZINC000005882138
PDB chain1jut Chain B Residue 305 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1jut Multi-targeted antifolates aimed at avoiding drug resistance form covalent closed inhibitory complexes with human and Escherichia coli thymidylate synthases.
Resolution2.7 Å
Binding residue
(original residue number in PDB)		W80 G173 F176 V262
Binding residue
(residue number reindexed from 1)		W80 G173 F176 V262
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=7.32,Ki=47.7nM
Enzymatic activity
Catalytic site (original residue number in PDB) E58 W80 Y94 C146 R166 D169 P175
Catalytic site (residue number reindexed from 1) E58 W80 Y94 C146 R166 D169 P175
Enzyme Commision number 2.1.1.45: thymidylate synthase.
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003723 RNA binding
GO:0004799 thymidylate synthase activity
GO:0008168 methyltransferase activity
GO:0016741 transferase activity, transferring one-carbon groups
GO:0042803 protein homodimerization activity
Biological Process
GO:0006231 dTMP biosynthetic process
GO:0006235 dTTP biosynthetic process
GO:0006417 regulation of translation
GO:0009165 nucleotide biosynthetic process
GO:0009314 response to radiation
GO:0032259 methylation
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1jut, PDBe:1jut, PDBj:1jut
PDBsum1jut
PubMed11697906
UniProtP0A884|TYSY_ECOLI Thymidylate synthase (Gene Name=thyA)

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