Structure of PDB 4foa Chain B

Receptor sequence
>4foaB (length=258) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
MTPYEDLLRFVLETGTPKSDTGTRSLFGQQMRYDLSAGFPLLTTKKVHFK
SVAYELLWFLRGDSNIGWLHEHGVTIWDEWASDTGELGPIYGVQWRSWPA
PSGEHIDQISAALDLLRTDPDSRRIIVSAWNVGEIERMALPPCHAFFQFY
VADGRLSCQLYQRSADLFLGVPFNIASYALLTHMMAAQAGLSVGEFIWTG
GDCHIYDNHVEQVRLQLSREPRPYPKLLLADRDSIFEYTYEDIVVKNYDP
HPAIKAPV
3D structure
PDB4foa Crystal structure of binary and ternary complexes of thymidylate synthase (ThyA) from Mycobacterium tuberculosis: Insights into the selectivity and mode of inhibition
ChainB
Resolution2.253 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E58 W80 Y94 C146 R166 D169
Catalytic site (residue number reindexed from 1) E55 W77 Y91 C143 R163 D166
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 B R126 R127 R123 R124
BS02 UFP B C146 Q165 R166 S167 D169 N177 H207 Y209 C143 Q162 R163 S164 D166 N174 H204 Y206
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
GO:0046079 dUMP catabolic process
GO:0046677 response to antibiotic
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Cellular Component
External links
PDB RCSB:4foa, PDBe:4foa, PDBj:4foa
PDBsum4foa
PubMed
UniProtP9WFR9|TYSY_MYCTU Thymidylate synthase ThyA (Gene Name=thyA)

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