Structure of PDB 2bbq Chain B Binding Site BS03

Receptor Information
>2bbq 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 IDPFG
InChIInChI=1S/C39H44N8O15/c1-2-17-47(19-20-3-8-24-23(18-20)34(54)46-39(40)45-24)22-6-4-21(5-7-22)33(53)44-28(38(61)62)11-15-31(50)42-26(36(57)58)9-13-29(48)41-25(35(55)56)10-14-30(49)43-27(37(59)60)12-16-32(51)52/h1,3-8,18,25-28H,9-17,19H2,(H,41,48)(H,42,50)(H,43,49)(H,44,53)(H,51,52)(H,55,56)(H,57,58)(H,59,60)(H,61,62)(H3,40,45,46,54)/t25-,26-,27?,28-/m0/s1
InChIKeySASAWWASHFSVQE-QGMKSFRFSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C#CCN(Cc1ccc2c(c1)C(=O)N=C(N2)N)c3ccc(cc3)C(=O)NC(CCC(=O)NC(CCC(=O)NC(CCC(=O)NC(CCC(=O)O)C(=O)O)C(=O)O)C(=O)O)C(=O)O
CACTVS 3.341NC1=NC(=O)c2cc(CN(CC#C)c3ccc(cc3)C(=O)N[C@@H](CCC(=O)N[C@@H](CCC(=O)N[C@@H](CCC(=O)NC(CCC(O)=O)C(O)=O)C(O)=O)C(O)=O)C(O)=O)ccc2N1
CACTVS 3.341NC1=NC(=O)c2cc(CN(CC#C)c3ccc(cc3)C(=O)N[CH](CCC(=O)N[CH](CCC(=O)N[CH](CCC(=O)NC(CCC(O)=O)C(O)=O)C(O)=O)C(O)=O)C(O)=O)ccc2N1
OpenEye OEToolkits 1.5.0C#CC[N@](Cc1ccc2c(c1)C(=O)N=C(N2)N)c3ccc(cc3)C(=O)N[C@@H](CCC(=O)N[C@@H](CCC(=O)N[C@@H](CCC(=O)N[C@H](CCC(=O)O)C(=O)O)C(=O)O)C(=O)O)C(=O)O
ACDLabs 10.04O=C(O)C(NC(=O)CCC(C(=O)O)NC(=O)CCC(C(=O)O)NC(=O)CCC(C(=O)O)NC(=O)c1ccc(cc1)N(CC#C)Cc2ccc3NC(=NC(=O)c3c2)N)CCC(=O)O
FormulaC39 H44 N8 O15
Name10-PARPARGYL-5,8-DIDEAZAFOLATE-4-GLUTAMIC ACID
ChEMBL
DrugBank
ZINC
PDB chain2bbq Chain B Residue 532 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2bbq Structural basis for recognition of polyglutamyl folates by thymidylate synthase.
Resolution2.3 Å
Binding residue
(original residue number in PDB)		H51 I79 W80 W83 D169 G173 F176 N177
Binding residue
(residue number reindexed from 1)		H51 I79 W80 W83 D169 G173 F176 N177
Annotation score1
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

View graph for
Molecular Function
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Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2bbq, PDBe:2bbq, PDBj:2bbq
PDBsum2bbq
PubMed1390771
UniProtP0A884|TYSY_ECOLI Thymidylate synthase (Gene Name=thyA)

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