Structure of PDB 1tsz Chain A

Receptor sequence
>1tszA (length=316) Species: 1582 (Lacticaseibacillus casei) [Search protein sequence]
MLEQPYLDLAKKVLDEGHFKPDRTHTGTYSIFGHQMRFDLSKGFPLLTTK
KVPFGLIKSELLWFLHGDTNIRFLLQHRNHIWDEWAFEKWVKSDEYHGPD
MTDFGHRSQKDPEFAAVYHEEMAKFDDRVLHDDAFAAKYGDLGLVYGSQW
RAWHTSKGDTIDQLGDVIEQIKTHPYSRKLIVSAWNPEDVPTMALPPCHT
LYQFYVNDGKLSLQLYQRSADIFLGVPFNIASYALLTHLVAHECGLEVGE
FIHTFGDAHLYVNHLDQIKEQLSRTPRPAPTLQLNPDKHDIFDFDMKDIK
LLNYDPYPAIKAPVAV
3D structure
PDB1tsz Contribution of a salt bridge to binding affinity and dUMP orientation to catalytic rate: mutation of a substrate-binding arginine in thymidylate synthase.
ChainA
Resolution2.75 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 PO4 A R23 R218 R23 R218
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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Biological Process
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Cellular Component
External links
PDB RCSB:1tsz, PDBe:1tsz, PDBj:1tsz
PDBsum1tsz
PubMed9053905
UniProtP00469|TYSY_LACCA Thymidylate synthase (Gene Name=thyA)

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