Structure of PDB 3bfi Chain A

Receptor sequence
>3bfiA (length=264) Species: 562 (Escherichia coli) [Search protein sequence]
MKQYLELMQKVLDEGTQKNDRTGTGTLSIFGHQMRFNLQDGFPLVTTKRC
HLRSIIHELLWFLQGDTNIAYLHENNVTIWDEWADENGDLGPVYGKQWRA
WPTPDGRHIDQITTVLNQLKNDPDSRRIIVSAWNVGELDKMALAPCHAFF
QFYVADGKLSCQLYQRSCDVFLGLPFNIASYALLVHMMAQQCDLEVGDFV
WTGGDTHLMSNHMDQTHLQLSREPRPLPKLIIKRKPESIFDYRFEDFEIE
GYDPHPGIKAPVAI
3D structure
PDB3bfi E.Coli thymidylate synthase complexed with 5-NITRO-2'-DEOXY URIDINE
ChainA
Resolution2.2 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
Catalytic site (residue number reindexed from 1) E58 W80 Y94 C146 R166 D169
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 NDU A R21 Y94 C146 Q165 R166 S167 C168 D169 N177 H207 R21 Y94 C146 Q165 R166 S167 C168 D169 N177 H207
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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Cellular Component
External links
PDB RCSB:3bfi, PDBe:3bfi, PDBj:3bfi
PDBsum3bfi
PubMed
UniProtP0A884|TYSY_ECOLI Thymidylate synthase (Gene Name=thyA)

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