Structure of PDB 2af6 Chain E

Receptor sequence
>2af6E (length=243) Species: 1773 (Mycobacterium tuberculosis) [Search protein sequence]
ETAPLRVQLIAKTDFLAPPDVPWTTDADGGPALVEFAGRACYQSWSKPNP
KTATNAGYLRHIMDVGHFSVLEHASVSFYITGISRSCTHELIRHRHFSYS
QLSQRYVPEKDSRVVVPPGMEDDADLRHILTEAADAARATYSELLAKLEA
KFADQPNAILRRKQARQAARAVMPNATETRIVVTGNYRAWRHFIAMRASE
HADVEIRRLAIECLRQLAAVAPAVFADFEVTTLADGTEVATSP
3D structure
PDB2af6 Structure of the Mycobacterium tuberculosis Flavin Dependent Thymidylate Synthase (MtbThyX) at 2.0A Resolution.
ChainE
Resolution2.01 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.1.1.148: thymidylate synthase (FAD).
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 FAD E R95 H96 R97 H98 H194 R199 H203 R93 H94 R95 H96 H192 R197 H201
BS02 BRU E H91 E92 R95 R199 H89 E90 R93 R197
BS03 FAD E C43 S71 E74 H98 N188 R190 C41 S69 E72 H96 N186 R188
BS04 FAD E S102 Q103 S100 Q101
BS05 BRU E R87 Q103 S105 Q106 R107 Y108 R172 R85 Q101 S103 Q104 R105 Y106 R170
Gene Ontology
Molecular Function
GO:0004799 thymidylate synthase activity
GO:0008168 methyltransferase activity
GO:0050660 flavin adenine dinucleotide binding
GO:0050797 thymidylate synthase (FAD) activity
GO:0070402 NADPH binding
Biological Process
GO:0006231 dTMP biosynthetic process
GO:0006235 dTTP biosynthetic process
GO:0009165 nucleotide biosynthetic process
GO:0032259 methylation

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Molecular Function
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Biological Process
External links
PDB RCSB:2af6, PDBe:2af6, PDBj:2af6
PDBsum2af6
PubMed16139296
UniProtP9WG57|THYX_MYCTU Flavin-dependent thymidylate synthase (Gene Name=thyX)

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