Structure of PDB 1bdu Chain A

Receptor sequence

>1bduA (length=264) Species: 562 (Escherichia coli)

MKQYLELMQKVLDEGTQKNDRTGTGTLSIFGHQMRFNLQDGFPLVTTKRC
HLRSIIHELLWFLQGDTNIAYLHENNVTIWDEWADENGDLGPVYGKQWRA
WPTPDGRHIDQITTVLNQLKNDPDSRRIIVSAWNVGELDKMALAPCHAFF
QFYVADGKLSCQLYQRSCDVFLGLPFNIASYALLVHMMAQQCDLEVGDFV
WTGGDTHLYSNHMDQTHLQLSREPRPLPKLIIKRKPESIFDYRFEDFEIE
GYDPHPGIKAPVAI

3D structure

• PDB: 1bdu The additivity of substrate fragments in enzyme-ligand binding.
• Chain: A
• Resolution: 2.1 Å

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	DUR	A	C146 S167 C168 D169 N177 H207 Y209	C146 S167 C168 D169 N177 H207 Y209

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

External links

• PDB: RCSB:1bdu, PDBe:1bdu, PDBj:1bdu
• PDBsum: 1bdu
• PubMed: 9687366
• UniProt: P0A884|TYSY_ECOLI Thymidylate synthase (Gene Name=thyA)