Structure of PDB 1nce Chain B

Receptor sequence

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

MKQYLELMQKVLDEGTQKNDRTGTGTLSIFGHQMRFNLQDGFPLVTTKRC
HLRSIIHELLWFLQGDTNIAYLHENNVTIWDEWADENGDLGPVYGKQWRA
WPTPDGRHIDQITTVLNQLKNDPDSRRIIVSAWNVGELDKMALAPCHAFF
QFYVADGKLSCQLYQRSCCVFLGLPFNIASYALLVHMMAQQCDLEVGDFV
WTGGDTHLYSNHMDQTHLQLSREPRPLPKLIIKRKPESIFDYRFEDFEIE
GYDPHPGIKAPVAI

3D structure

• PDB: 1nce The only active mutant of thymidylate synthase D169, a residue far from the site of methyl transfer, demonstrates the exquisite nature of enzyme specificity.
• Chain: B
• Resolution: 2.4 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): E58 W80 Y94 C146 R166 C169
• Catalytic site (residue number reindexed from 1): E58 W80 Y94 C146 R166 C169
• 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	B	R126 R127	R126 R127
BS02	UMP	B	C146 H147 Q165 R166 S167 C168 C169 N177 H207 Y209	C146 H147 Q165 R166 S167 C168 C169 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:1nce, PDBe:1nce, PDBj:1nce
• PDBsum: 1nce
• PubMed: 12702803
• UniProt: P0A884|TYSY_ECOLI Thymidylate synthase (Gene Name=thyA)