Structure of PDB 1bp0 Chain A

Receptor sequence
>1bp0A (length=316) Species: 1582 (Lacticaseibacillus casei) [Search protein sequence]
MLEQPYLDLAKKVLDEGHFKPDITHTGTYSIFGHQMRFDLSKGFPLLTTK
KVPFGLIKSELLWFLHGDTNIRFLLQHRNHIWDEWAFEKWVKSDEYHGPD
MTDFGHRSQKDPEFAAVYHEEMAKFDDRVLHDDAFAAKYGDLGLVYGSQW
RAWHTSKGDTIDQLGDVIEQIKTHPYSRRLIVSAWNPEDVPTMALPPCHT
LYQFYVNDGKLSLQLYQRSADIFLGVPFNIASYALLTHLVAHECGLEVGE
FIHTFGDAHLYVNHLDQIKEQLSRTPRPAPTLQLNPDKHDIFDFDMKDIK
LLNYDPYPAIKAPVAV
3D structure
PDB1bp0 Energetic contributions of four arginines to phosphate-binding in thymidylate synthase are more than additive and depend on optimization of "effective charge balance".
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 C198 H199 R218 S219 A220 D221 N229 H259 Y261 C198 H199 R218 S219 A220 D221 N229 H259 Y261 MOAD: Kd=4uM
PDBbind-CN: -logKd/Ki=5.40,Kd=4.0uM
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

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Molecular Function
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Cellular Component
External links
PDB RCSB:1bp0, PDBe:1bp0, PDBj:1bp0
PDBsum1bp0
PubMed10653645
UniProtP00469|TYSY_LACCA Thymidylate synthase (Gene Name=thyA)

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