Structure of PDB 1bpj Chain A

Receptor sequence

>1bpjA (length=316) Species: 1582 (Lacticaseibacillus casei)

MLEQPYLDLAKKVLDEGHFKPDRTHTGTYSIFGHQMRFDLSKGFPLLTTK
KVPFGLIKSELLWFLHGDTNIRFLLQHRNHIWDEWAFEKWVKSDEYHGPD
MTDFGHRSQKDPEFAAVYHEEMAKFDDRVLHDDAFAAKYGDLGLVYGSQW
RAWHTSKGDTIDQLGDVIEQIKTHPYSTTLIVSAWNPEDVPTMALPPCHT
LYQFYVNDGKLSLQLYQRSADIFLGVPFNIASYALLTHLVAHECGLEVGE
FIHTFGDAHLYVNHLDQIKEQLSRTPRPAPTLQLNPDKHDIFDFDMKDIK
LLNYDPYPAIKAPVAV

3D structure

• PDB: 1bpj Energetic contributions of four arginines to phosphate-binding in thymidylate synthase are more than additive and depend on optimization of "effective charge balance".
• Chain: A
• Resolution: 2.4 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): E60 W82 Y146 C198 R218 D221
• Catalytic site (residue number reindexed from 1): E60 W82 Y146 C198 R218 D221
• 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	R23 S219 A220 D221 N229 H259 Y261	R23 S219 A220 D221 N229 H259 Y261

Gene Ontology

Molecular Function

• GO:0004799 thymidylate synthase activity
• GO:0008168 methyltransferase activity
• GO:0016741 transferase activity, transferring one-carbon groups

Biological Process

• GO:0006231 dTMP biosynthetic process
• GO:0006235 dTTP biosynthetic process
• GO:0009165 nucleotide biosynthetic process
• GO:0032259 methylation

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol

External links

• PDB: RCSB:1bpj, PDBe:1bpj, PDBj:1bpj
• PDBsum: 1bpj
• PubMed: 10653645
• UniProt: P00469|TYSY_LACCA Thymidylate synthase (Gene Name=thyA)