Structure of PDB 2bbq Chain A

Receptor sequence
>2bbqA (length=264) Species: 562 (Escherichia coli) [Search protein sequence]
MKQYLELMQKVLDEGTQKNDRTGTGTLSIFGHQMRFNLQDGFPLVTTKRC
HLRSIIHELLWFLQGDTNIAYLHENNVTIWDEWADENGDLGPVYGKQWRA
WPTPDGRHIDQITTVLNQLKNDPDSRRIIVSAWNVGELDKMALAPCHAFF
QFYVADGKLSCQLYQRSCDVFLGLPFNIASYALLVHMMAQQCDLEVGDFV
WTGGDTHLYSNHMDQTHLQLSREPRPLPKLIIKRKPESIFDYRFEDFEIE
GYDPHPGIKAPVAI
3D structure
PDB2bbq Structural basis for recognition of polyglutamyl folates by thymidylate synthase.
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 UMP A R21 C146 H147 Q165 R166 S167 D169 N177 H207 Y209 R21 C146 H147 Q165 R166 S167 D169 N177 H207 Y209
BS02 PFG A H51 R53 I79 W80 W83 L143 D169 G173 F176 N177 Y209 A263 H51 R53 I79 W80 W83 L143 D169 G173 F176 N177 Y209 A263
BS03 UMP A R126 R127 R126 R127
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:2bbq, PDBe:2bbq, PDBj:2bbq
PDBsum2bbq
PubMed1390771
UniProtP0A884|TYSY_ECOLI Thymidylate synthase (Gene Name=thyA)

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