Structure of PDB 6qxs Chain D

Receptor sequence
>6qxsD (length=315) Species: 1351 (Enterococcus faecalis) [Search protein sequence]
MEEAYLALGKKILEEGHFKEDRTGTGTYSLFGYQMRFDLAKGFPLLTTKR
VPFGLIKSELLWFLKGDTNIRYLLERNNHIWDEWAFERYVKSADYQGPDM
TDFGHRVLQDPAFAEQYKEEHQKFCDAILNDAEFAEKYGELGNIYGAQWR
HWETKDGSFIDQLANVIEMIKTNPDSRRLIVSAWNPEDVPSMALPPCHTM
FQFYVNEGKLSCQLYQRSADVFLGVPFNIASYALLTHLIAHETGLEVGEF
VHTLGDAHLYQNHVEQMQEQLSREVRSFPTLVLNPDKASVFDFDMEDIKV
EGYDPHPTIKAPIAV
3D structure
PDB6qxs Structural Comparison ofEnterococcus faecalisand Human Thymidylate Synthase Complexes with the Substrate dUMP and Its Analogue FdUMP Provides Hints about Enzyme Conformational Variabilities.
ChainD
Resolution2.88 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E59 W81 Y145 C197 R217 D220
Catalytic site (residue number reindexed from 1) E59 W81 Y145 C197 R217 D220
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 UFP D R22 Y145 C197 H198 R217 S218 D220 H258 Y260 R22 Y145 C197 H198 R217 S218 D220 H258 Y260
BS02 FFO D I80 W81 W84 D220 I313 A314 I80 W81 W84 D220 I313 A314
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:6qxs, PDBe:6qxs, PDBj:6qxs
PDBsum6qxs
PubMed30935102
UniProtQ834R3|TYSY_ENTFA Thymidylate synthase (Gene Name=thyA)

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