Structure of PDB 1fwm Chain A

Receptor sequence

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

MKQYLELMQKVLDEGTQKNDRTGTGTLSIFGHQMRFNLQDGFPLVTTKRC
HLRSIIHELLWFLQGDTNIAYLHENNVTIWDEWADENGDLGPVYGKQWRA
WPTPDGRHIDQITTVLNQLKNDPDSRRIIVSAWNVGELDKMALAPCHAFF
QFYVADGKLSCQLYQQSCDVFLGLPFNIASYALLVHMMAQQCDLEVGDFV
WTGGDTHLYSNHMDQTHLQLSREPRPLPKLIIKRKPESIFDYRFEDFEIE
GYDPHPGIKAPVAI

3D structure

• PDB: 1fwm Crystal structures of thymidylate synthase mutant R166Q: Structural basis for the nearly complete loss of catalytic activity.
• Chain: A
• Resolution: 2.2 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Y94 C146 Q166 D169
• Catalytic site (residue number reindexed from 1): Y94 C146 Q166 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	SO4	A	R21 S167	R21 S167

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:1fwm, PDBe:1fwm, PDBj:1fwm
• PDBsum: 1fwm
• PubMed: 16615077
• UniProt: P0A884|TYSY_ECOLI Thymidylate synthase (Gene Name=thyA)